Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3 (402 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2002 Feb; 11(2): 262-270.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.546, 5-year impact factor: 3.029
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0036147722&partnerID=40&md5=77b3edf66ab11034226069ba144aadfa
Keywords: Collagen, Proline, Protein Structure Stability, Triple Helix, X-Ray Structure, Collagen Fibril, Glycine, Hydroxyproline, Polypeptide, Article, Crystal Structure, Diffraction, Electricity, Gravity, Molecular Model, Priority Journal, Protein Assembly, Protein Stability, Synchrotron Radiation, Crystallization, Crystallography, Hydrogen Bonding, Oligopeptides, Protein Conformation,
Affiliations:
*** IBB - CNR ***
Centro di Studio di Biocristallografia, CNR, I-80134 Napoli, Italy
Dipartimento di Chimica, Università degli Studi di Napoli Federico II, I-80126, Napoli, Italy
CEINGE, Biotecnologie Avanzate Scarl, Napoli, Italy
References:
Bella, J., Brodsky, B., Berman, H.M., Hydration structure of a collagen peptide (1995) Structure, 3, pp. 893-90
Bella, J., Eaton, M., Brodsky, B., Berman, H.M., Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution (1994) Science, 266, pp. 75-81
Berisio, R., Vitagliano, L., Mazzarella, L., Zagari, A., Crystal structure determination of the collagen-like polypeptide with repeating sequence Pro-Hyp-Gly: Implications for hydration (2001) Biopolymers, 56, pp. 8-13
Berman, H.M., Bhat, T.N., Bourne, P.E., Feng, Z., Gilliland, G., Weissig, H., Westbrook, J., The protein data bank and the challenge of structural genomics (2000) Nat. Struct. Biol., 7, pp. 957-959
Bretscher, L.E., Jenkins, C.L., Taylor, K.M., DeRider, M.L., Raines, R.T., Conformational stability of collagen relies on a stereoelectronic effect (2001) J. Am. Chem. Soc., 123, pp. 777-778
Esnouf, R.M., Further additions to MolScript version 1.4, including reading and contouring of electron-density maps (1999) Acta Crystallogr. D, 55, pp. 938-940
Esposito, L., Vitagliano, L., Sica, F., Sorrentino, G., Zagari, A., Mazzarella, L., The ultrahigh resolution crystal structure of ribonuclease A containing an isoaspartyl residue: Hydration and sterochemical analysis (2000) J. Mol. Biol., 297, pp. 713-732
Fields, G.B., Prockop, D.J., Perspectives on the synthesis and application of triple-helical, collagen-model peptides (1996) Biopolymers, 40, pp. 345-357
Finney, J.L., Gellatly, B.J., Golton, I.C., Goodfellow, J., Solvent effects and polar interactions in the structural stability and dynamics of globular proteins (1980) Biophys. J., 32, pp. 17-33
Fraser, R.D.B., MacRae, T.P., Suzuki, E., Chain conformation in the collagen molecule (1979) J. Mol. Biol., 129, pp. 463-481
Holmgren, S.K., Bretscher, L.E., Taylor, K.M., Raines, R.T., A hyperstable collagen mimic (1999) Chem. Biol., 6, pp. 63-70
Holmgren, S.K., Taylor, K.M., Bretscher, L.E., Raines, R.T., Code for collagen's stability deciphered (1998) Nature, 392, pp. 666-667
Improta, R., Benzi, C., Barone, V., Understanding the role of stereoelectronic effects in determining collagen stability. I. A quantum mechanical study of proline, hydroxyproline and fluoroproline dipeptide analogues in aqueous solution (2001) J. Am. Chem. Soc., , in press
Inouye, K., Kobayashi, Y., Kyogoku, Y., Kishida, Y., Sakakibara, S., Prockop, D.J., Synthesis and physical properties of (hydroxyprolineproline-glycine)10: Hydroxyproline in the x-position decreases the melting temperature of the collagen triple helix (1982) Arch. Biochem. Biophys., 219, pp. 198-203
Jones, E.Y., Miller, A., Analysis of structural design features in collagen (1991) J. Mol. Biol., 218, pp. 209-219
Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M., Improved methods for binding protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. A, 47, pp. 110-119
Kramer, R.Z., Bella, J., Mayville, P., Brodsky, B., Berman, H.M., Sequence dependent conformational variations of collagen triple-helical structure (1999) Nat. Struct. Biol., 6, pp. 454-457
Kramer, R.Z., Venugopal, M.G., Bella, J., Mayville, P., Brodsky, B., Berman, H.M., Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair (2000) J. Mol. Biol., 301, pp. 1191-1205
Kramer, R.Z., Vitagliano, L., Bella, J., Berisio, R., Mazzarella, L., Brodsky, B., Zagari, A., Berman, H.M., X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly) (1998) J. Mol. Biol., 280, pp. 623-638
Kraulis, P.J., MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures (1991) J. Appl. Crystallogr., 24, pp. 946-950
Melacini, G., Bonvin, A.M., Goodman, M., Boelens, R., Kaptein, R., Hydration dynamics of the collagen triple helix by NMR (2000) J. Mol. Biol., 300, pp. 1041-1049
Merritt, E.A., Bacon, D.J., Raster3D: Photorealistic molecular graphics (1997) Methods Enzymol., 277, pp. 505-524
Miller, M.H., Nemethy, G., Scheraga, H., Calculation of the structures of collagen models. Role of interchain interactions in determining the triplehelical coiled-coil conformation. 2. Poly(glycyl-prolyl-hydroxyprolyl) (1980) Macromolecules, 13, pp. 470-478
Miller, M.H., Scheraga, H.A., Calculation of the structures of collagen models. Role of interchain interactions in determining the triple-helical coiled-coil conformation. I. Poly(glycyl-prolyl-prolyl) (1976) J. Polym. Sci., 54, pp. 171-200
Murshudov, G.N., Vagin, A.A., Lebedev, A., Wilson, K.S., Dodson, E.J., Efficient anisotropic refinement of macromolecular structures using FFT (1999) Acta Crystallogr. D, 55, pp. 247-255
Nagarajan, V., Kamitori, S., Okuyama, K., Crystal structure analysis of collagen model peptide (Pro-Pro-Gly)10 (1998) J. Biochem., 124, pp. 1117-1123
Navaza, J., AMoRe, an automated package for molecular replacement (1994) Acta Crystallogr. A, 50, pp. 157-163
Némethy, G., Gibson, K.D., Palmer, K.A., Yoon, C.N., Paterlini, G., Zagari, A., Rumsey, S., Scheraga, H.A., Energy parameters in polypeptides. 10. Improved geometrical parameters and nonbonded interactions for use in ECEPP/3 algoritm, with application to proline-containing peptides (1992) J. Phys. Chem., 96, pp. 6472-6484
Nicholls, A., Sharp, K.A., Honig, B., Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons (1991) Proteins, 11, pp. 281-296
Okuyama, K., Arnott, S., Takayanagi, M., Kakudo, M., Crystal and molecular structure of a collagen-like polypeptide (Pro-Pro-Gly)10 (1981) J. Mol. Biol., 152, pp. 427-443
Okuyama, K., Nagarajan, V., Kamitori, S., 7/2-Helical model for collagen - Evidence from model peptides (1999) Proc. Indian Acad. Sci., Chem. Sci., 111, pp. 19-34
Okuyama, K., Takayanagi, M., Ashida, T., Kakudo, M., A new structural model for collagen (1977) Polym. J., 9, pp. 341-343
Otwinowsky, Z., Minor, W., Processing of x-ray diffraction data collected in oscillation mode (1997) Methods Enzymol., 276, pp. 307-326
Perrakis, A., Morris, R., Lamzin, V.S., Automated protein model building combined with iteractive structure refinement (1999) Nat. Struct. Biol., 6, pp. 458-463
Persikov, A.V., Ramshaw, J.A., Kirkpatrick, A., Brodsky, B., Amino acid propensities for the collagen triple-helix (2000) Biochemistry, 39, pp. 14960-14967
Ramshaw, J.A., Shah, N.K., Brodsky, B., Gly-X-Y tripeptide frequencies in collagen: A context for host-guest triple-helical peptides (1998) J. Struct. Biol., 122, pp. 86-91
Rich, A., Crick, F.H., The molecular structure of collagen (1961) J. Mol. Biol., 3, pp. 483-506
Sheldrick, G.M., Schneider, T.R., SHELXL: High-resolution refinement (1997) Methods Enzymol., 277, pp. 319-343
Vitagliano, L., Berisio, R., Mazzarella, L., Zagari, A., Structural bases of collagen stabilization induced by proline hydroxylation (2001) Biopolymers, 36, pp. 459-464
Yonath, A., Traub, W., Polymers of tripeptides as collagen models. IV. Structure analysis of poly(L-proly-glycyl-L-proline) (1969) J. Mol. Biol., 43, pp. 461-477
Berman, H. M., Bhat, T. N., Bourne, P. E., Feng, Z., Gilliland, G., Weissig, H., Westbrook, J., The protein data bank and the challenge of structural genomics (2000) Nat. Struct. Biol., 7, pp. 957-959
Bretscher, L. E., Jenkins, C. L., Taylor, K. M., DeRider, M. L., Raines, R. T., Conformational stability of collagen relies on a stereoelectronic effect (2001) J. Am. Chem. Soc., 123, pp. 777-778
Esnouf, R. M., Further additions to MolScript version 1. 4, including reading and contouring of electron-density maps (1999) Acta Crystallogr. D, 55, pp. 938-940
Fields, G. B., Prockop, D. J., Perspectives on the synthesis and application of triple-helical, collagen-model peptides (1996) Biopolymers, 40, pp. 345-357
Finney, J. L., Gellatly, B. J., Golton, I. C., Goodfellow, J., Solvent effects and polar interactions in the structural stability and dynamics of globular proteins (1980) Biophys. J., 32, pp. 17-33
Fraser, R. D. B., MacRae, T. P., Suzuki, E., Chain conformation in the collagen molecule (1979) J. Mol. Biol., 129, pp. 463-481
Holmgren, S. K., Bretscher, L. E., Taylor, K. M., Raines, R. T., A hyperstable collagen mimic (1999) Chem. Biol., 6, pp. 63-70
Holmgren, S. K., Taylor, K. M., Bretscher, L. E., Raines, R. T., Code for collagen's stability deciphered (1998) Nature, 392, pp. 666-667
Jones, E. Y., Miller, A., Analysis of structural design features in collagen (1991) J. Mol. Biol., 218, pp. 209-219
Jones, T. A., Zou, J. Y., Cowan, S. W., Kjeldgaard, M., Improved methods for binding protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. A, 47, pp. 110-119
Kramer, R. Z., Bella, J., Mayville, P., Brodsky, B., Berman, H. M., Sequence dependent conformational variations of collagen triple-helical structure (1999) Nat. Struct. Biol., 6, pp. 454-457
Kramer, R. Z., Venugopal, M. G., Bella, J., Mayville, P., Brodsky, B., Berman, H. M., Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair (2000) J. Mol. Biol., 301, pp. 1191-1205
Kramer, R. Z., Vitagliano, L., Bella, J., Berisio, R., Mazzarella, L., Brodsky, B., Zagari, A., Berman, H. M., X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly) (1998) J. Mol. Biol., 280, pp. 623-638
Kraulis, P. J., MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures (1991) J. Appl. Crystallogr., 24, pp. 946-950
Merritt, E. A., Bacon, D. J., Raster3D: Photorealistic molecular graphics (1997) Methods Enzymol., 277, pp. 505-524
Miller, M. H., Nemethy, G., Scheraga, H., Calculation of the structures of collagen models. Role of interchain interactions in determining the triplehelical coiled-coil conformation. 2. Poly (glycyl-prolyl-hydroxyprolyl) (1980) Macromolecules, 13, pp. 470-478
Miller, M. H., Scheraga, H. A., Calculation of the structures of collagen models. Role of interchain interactions in determining the triple-helical coiled-coil conformation. I. Poly (glycyl-prolyl-prolyl) (1976) J. Polym. Sci., 54, pp. 171-200
Murshudov, G. N., Vagin, A. A., Lebedev, A., Wilson, K. S., Dodson, E. J., Efficient anisotropic refinement of macromolecular structures using FFT (1999) Acta Crystallogr. D, 55, pp. 247-255
N methy, G., Gibson, K. D., Palmer, K. A., Yoon, C. N., Paterlini, G., Zagari, A., Rumsey, S., Scheraga, H. A., Energy parameters in polypeptides. 10. Improved geometrical parameters and nonbonded interactions for use in ECEPP/3 algoritm, with application to proline-containing peptides (1992) J. Phys. Chem., 96, pp. 6472-6484
Persikov, A. V., Ramshaw, J. A., Kirkpatrick, A., Brodsky, B., Amino acid propensities for the collagen triple-helix (2000) Biochemistry, 39, pp. 14960-14967
Ramshaw, J. A., Shah, N. K., Brodsky, B., Gly-X-Y tripeptide frequencies in collagen: A context for host-guest triple-helical peptides (1998) J. Struct. Biol., 122, pp. 86-91
Sheldrick, G. M., Schneider, T. R., SHELXL: High-resolution refinement (1997) Methods Enzymol., 277, pp. 319-343
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2002 Feb; 11(2): 262-270.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.546, 5-year impact factor: 3.029
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0036147722&partnerID=40&md5=77b3edf66ab11034226069ba144aadfa
Keywords: Collagen, Proline, Protein Structure Stability, Triple Helix, X-Ray Structure, Collagen Fibril, Glycine, Hydroxyproline, Polypeptide, Article, Crystal Structure, Diffraction, Electricity, Gravity, Molecular Model, Priority Journal, Protein Assembly, Protein Stability, Synchrotron Radiation, Crystallization, Crystallography, Hydrogen Bonding, Oligopeptides, Protein Conformation,
Affiliations:
*** IBB - CNR ***
Centro di Studio di Biocristallografia, CNR, I-80134 Napoli, Italy
Dipartimento di Chimica, Università degli Studi di Napoli Federico II, I-80126, Napoli, Italy
CEINGE, Biotecnologie Avanzate Scarl, Napoli, Italy
References:
Bella, J., Brodsky, B., Berman, H.M., Hydration structure of a collagen peptide (1995) Structure, 3, pp. 893-90
Bella, J., Eaton, M., Brodsky, B., Berman, H.M., Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution (1994) Science, 266, pp. 75-81
Berisio, R., Vitagliano, L., Mazzarella, L., Zagari, A., Crystal structure determination of the collagen-like polypeptide with repeating sequence Pro-Hyp-Gly: Implications for hydration (2001) Biopolymers, 56, pp. 8-13
Berman, H.M., Bhat, T.N., Bourne, P.E., Feng, Z., Gilliland, G., Weissig, H., Westbrook, J., The protein data bank and the challenge of structural genomics (2000) Nat. Struct. Biol., 7, pp. 957-959
Bretscher, L.E., Jenkins, C.L., Taylor, K.M., DeRider, M.L., Raines, R.T., Conformational stability of collagen relies on a stereoelectronic effect (2001) J. Am. Chem. Soc., 123, pp. 777-778
Esnouf, R.M., Further additions to MolScript version 1.4, including reading and contouring of electron-density maps (1999) Acta Crystallogr. D, 55, pp. 938-940
Esposito, L., Vitagliano, L., Sica, F., Sorrentino, G., Zagari, A., Mazzarella, L., The ultrahigh resolution crystal structure of ribonuclease A containing an isoaspartyl residue: Hydration and sterochemical analysis (2000) J. Mol. Biol., 297, pp. 713-732
Fields, G.B., Prockop, D.J., Perspectives on the synthesis and application of triple-helical, collagen-model peptides (1996) Biopolymers, 40, pp. 345-357
Finney, J.L., Gellatly, B.J., Golton, I.C., Goodfellow, J., Solvent effects and polar interactions in the structural stability and dynamics of globular proteins (1980) Biophys. J., 32, pp. 17-33
Fraser, R.D.B., MacRae, T.P., Suzuki, E., Chain conformation in the collagen molecule (1979) J. Mol. Biol., 129, pp. 463-481
Holmgren, S.K., Bretscher, L.E., Taylor, K.M., Raines, R.T., A hyperstable collagen mimic (1999) Chem. Biol., 6, pp. 63-70
Holmgren, S.K., Taylor, K.M., Bretscher, L.E., Raines, R.T., Code for collagen's stability deciphered (1998) Nature, 392, pp. 666-667
Improta, R., Benzi, C., Barone, V., Understanding the role of stereoelectronic effects in determining collagen stability. I. A quantum mechanical study of proline, hydroxyproline and fluoroproline dipeptide analogues in aqueous solution (2001) J. Am. Chem. Soc., , in press
Inouye, K., Kobayashi, Y., Kyogoku, Y., Kishida, Y., Sakakibara, S., Prockop, D.J., Synthesis and physical properties of (hydroxyprolineproline-glycine)10: Hydroxyproline in the x-position decreases the melting temperature of the collagen triple helix (1982) Arch. Biochem. Biophys., 219, pp. 198-203
Jones, E.Y., Miller, A., Analysis of structural design features in collagen (1991) J. Mol. Biol., 218, pp. 209-219
Jones, T.A., Zou, J.Y., Cowan, S.W., Kjeldgaard, M., Improved methods for binding protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. A, 47, pp. 110-119
Kramer, R.Z., Bella, J., Mayville, P., Brodsky, B., Berman, H.M., Sequence dependent conformational variations of collagen triple-helical structure (1999) Nat. Struct. Biol., 6, pp. 454-457
Kramer, R.Z., Venugopal, M.G., Bella, J., Mayville, P., Brodsky, B., Berman, H.M., Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair (2000) J. Mol. Biol., 301, pp. 1191-1205
Kramer, R.Z., Vitagliano, L., Bella, J., Berisio, R., Mazzarella, L., Brodsky, B., Zagari, A., Berman, H.M., X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly) (1998) J. Mol. Biol., 280, pp. 623-638
Kraulis, P.J., MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures (1991) J. Appl. Crystallogr., 24, pp. 946-950
Melacini, G., Bonvin, A.M., Goodman, M., Boelens, R., Kaptein, R., Hydration dynamics of the collagen triple helix by NMR (2000) J. Mol. Biol., 300, pp. 1041-1049
Merritt, E.A., Bacon, D.J., Raster3D: Photorealistic molecular graphics (1997) Methods Enzymol., 277, pp. 505-524
Miller, M.H., Nemethy, G., Scheraga, H., Calculation of the structures of collagen models. Role of interchain interactions in determining the triplehelical coiled-coil conformation. 2. Poly(glycyl-prolyl-hydroxyprolyl) (1980) Macromolecules, 13, pp. 470-478
Miller, M.H., Scheraga, H.A., Calculation of the structures of collagen models. Role of interchain interactions in determining the triple-helical coiled-coil conformation. I. Poly(glycyl-prolyl-prolyl) (1976) J. Polym. Sci., 54, pp. 171-200
Murshudov, G.N., Vagin, A.A., Lebedev, A., Wilson, K.S., Dodson, E.J., Efficient anisotropic refinement of macromolecular structures using FFT (1999) Acta Crystallogr. D, 55, pp. 247-255
Nagarajan, V., Kamitori, S., Okuyama, K., Crystal structure analysis of collagen model peptide (Pro-Pro-Gly)10 (1998) J. Biochem., 124, pp. 1117-1123
Navaza, J., AMoRe, an automated package for molecular replacement (1994) Acta Crystallogr. A, 50, pp. 157-163
Némethy, G., Gibson, K.D., Palmer, K.A., Yoon, C.N., Paterlini, G., Zagari, A., Rumsey, S., Scheraga, H.A., Energy parameters in polypeptides. 10. Improved geometrical parameters and nonbonded interactions for use in ECEPP/3 algoritm, with application to proline-containing peptides (1992) J. Phys. Chem., 96, pp. 6472-6484
Nicholls, A., Sharp, K.A., Honig, B., Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons (1991) Proteins, 11, pp. 281-296
Okuyama, K., Arnott, S., Takayanagi, M., Kakudo, M., Crystal and molecular structure of a collagen-like polypeptide (Pro-Pro-Gly)10 (1981) J. Mol. Biol., 152, pp. 427-443
Okuyama, K., Nagarajan, V., Kamitori, S., 7/2-Helical model for collagen - Evidence from model peptides (1999) Proc. Indian Acad. Sci., Chem. Sci., 111, pp. 19-34
Okuyama, K., Takayanagi, M., Ashida, T., Kakudo, M., A new structural model for collagen (1977) Polym. J., 9, pp. 341-343
Otwinowsky, Z., Minor, W., Processing of x-ray diffraction data collected in oscillation mode (1997) Methods Enzymol., 276, pp. 307-326
Perrakis, A., Morris, R., Lamzin, V.S., Automated protein model building combined with iteractive structure refinement (1999) Nat. Struct. Biol., 6, pp. 458-463
Persikov, A.V., Ramshaw, J.A., Kirkpatrick, A., Brodsky, B., Amino acid propensities for the collagen triple-helix (2000) Biochemistry, 39, pp. 14960-14967
Ramshaw, J.A., Shah, N.K., Brodsky, B., Gly-X-Y tripeptide frequencies in collagen: A context for host-guest triple-helical peptides (1998) J. Struct. Biol., 122, pp. 86-91
Rich, A., Crick, F.H., The molecular structure of collagen (1961) J. Mol. Biol., 3, pp. 483-506
Sheldrick, G.M., Schneider, T.R., SHELXL: High-resolution refinement (1997) Methods Enzymol., 277, pp. 319-343
Vitagliano, L., Berisio, R., Mazzarella, L., Zagari, A., Structural bases of collagen stabilization induced by proline hydroxylation (2001) Biopolymers, 36, pp. 459-464
Yonath, A., Traub, W., Polymers of tripeptides as collagen models. IV. Structure analysis of poly(L-proly-glycyl-L-proline) (1969) J. Mol. Biol., 43, pp. 461-477
Berman, H. M., Bhat, T. N., Bourne, P. E., Feng, Z., Gilliland, G., Weissig, H., Westbrook, J., The protein data bank and the challenge of structural genomics (2000) Nat. Struct. Biol., 7, pp. 957-959
Bretscher, L. E., Jenkins, C. L., Taylor, K. M., DeRider, M. L., Raines, R. T., Conformational stability of collagen relies on a stereoelectronic effect (2001) J. Am. Chem. Soc., 123, pp. 777-778
Esnouf, R. M., Further additions to MolScript version 1. 4, including reading and contouring of electron-density maps (1999) Acta Crystallogr. D, 55, pp. 938-940
Fields, G. B., Prockop, D. J., Perspectives on the synthesis and application of triple-helical, collagen-model peptides (1996) Biopolymers, 40, pp. 345-357
Finney, J. L., Gellatly, B. J., Golton, I. C., Goodfellow, J., Solvent effects and polar interactions in the structural stability and dynamics of globular proteins (1980) Biophys. J., 32, pp. 17-33
Fraser, R. D. B., MacRae, T. P., Suzuki, E., Chain conformation in the collagen molecule (1979) J. Mol. Biol., 129, pp. 463-481
Holmgren, S. K., Bretscher, L. E., Taylor, K. M., Raines, R. T., A hyperstable collagen mimic (1999) Chem. Biol., 6, pp. 63-70
Holmgren, S. K., Taylor, K. M., Bretscher, L. E., Raines, R. T., Code for collagen's stability deciphered (1998) Nature, 392, pp. 666-667
Jones, E. Y., Miller, A., Analysis of structural design features in collagen (1991) J. Mol. Biol., 218, pp. 209-219
Jones, T. A., Zou, J. Y., Cowan, S. W., Kjeldgaard, M., Improved methods for binding protein models in electron density maps and the location of errors in these models (1991) Acta Crystallogr. A, 47, pp. 110-119
Kramer, R. Z., Bella, J., Mayville, P., Brodsky, B., Berman, H. M., Sequence dependent conformational variations of collagen triple-helical structure (1999) Nat. Struct. Biol., 6, pp. 454-457
Kramer, R. Z., Venugopal, M. G., Bella, J., Mayville, P., Brodsky, B., Berman, H. M., Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair (2000) J. Mol. Biol., 301, pp. 1191-1205
Kramer, R. Z., Vitagliano, L., Bella, J., Berisio, R., Mazzarella, L., Brodsky, B., Zagari, A., Berman, H. M., X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly) (1998) J. Mol. Biol., 280, pp. 623-638
Kraulis, P. J., MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures (1991) J. Appl. Crystallogr., 24, pp. 946-950
Merritt, E. A., Bacon, D. J., Raster3D: Photorealistic molecular graphics (1997) Methods Enzymol., 277, pp. 505-524
Miller, M. H., Nemethy, G., Scheraga, H., Calculation of the structures of collagen models. Role of interchain interactions in determining the triplehelical coiled-coil conformation. 2. Poly (glycyl-prolyl-hydroxyprolyl) (1980) Macromolecules, 13, pp. 470-478
Miller, M. H., Scheraga, H. A., Calculation of the structures of collagen models. Role of interchain interactions in determining the triple-helical coiled-coil conformation. I. Poly (glycyl-prolyl-prolyl) (1976) J. Polym. Sci., 54, pp. 171-200
Murshudov, G. N., Vagin, A. A., Lebedev, A., Wilson, K. S., Dodson, E. J., Efficient anisotropic refinement of macromolecular structures using FFT (1999) Acta Crystallogr. D, 55, pp. 247-255
N methy, G., Gibson, K. D., Palmer, K. A., Yoon, C. N., Paterlini, G., Zagari, A., Rumsey, S., Scheraga, H. A., Energy parameters in polypeptides. 10. Improved geometrical parameters and nonbonded interactions for use in ECEPP/3 algoritm, with application to proline-containing peptides (1992) J. Phys. Chem., 96, pp. 6472-6484
Persikov, A. V., Ramshaw, J. A., Kirkpatrick, A., Brodsky, B., Amino acid propensities for the collagen triple-helix (2000) Biochemistry, 39, pp. 14960-14967
Ramshaw, J. A., Shah, N. K., Brodsky, B., Gly-X-Y tripeptide frequencies in collagen: A context for host-guest triple-helical peptides (1998) J. Struct. Biol., 122, pp. 86-91
Sheldrick, G. M., Schneider, T. R., SHELXL: High-resolution refinement (1997) Methods Enzymol., 277, pp. 319-343
Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3
The first report of the full-length structure of the collagen-like polypeptide [(Pro-Pro-Gly)10]3 is given. This structure was obtained from crystals grown in a microgravity environment, which diffracted up to 1.3 Å, using synchrotron radiation. The final model, which was refined to an Rfactor of 0.18, is the highest-resolution description of a collagen triple helix reported to date. This structure provides clues regarding a series of aspects related to collagen triple helix structure and assembly. The strict dependence of proline puckering on the position inside the Pro-Pro-Gly triplets and the correlation between backbone and side chain dihedral angles support the propensity-based mechanism of triple helix stabilization/destabilization induced by hydroxyproline. Furthermore, the analysis of [(Pro-Pro-Gly)10]3 packing, which is governed by electrostatic interactions, suggests that charges may act as locking features in the axial organization of triple helices in the collagen fibrils.
The first report of the full-length structure of the collagen-like polypeptide [(Pro-Pro-Gly)10]3 is given. This structure was obtained from crystals grown in a microgravity environment, which diffracted up to 1.3 Å, using synchrotron radiation. The final model, which was refined to an Rfactor of 0.18, is the highest-resolution description of a collagen triple helix reported to date. This structure provides clues regarding a series of aspects related to collagen triple helix structure and assembly. The strict dependence of proline puckering on the position inside the Pro-Pro-Gly triplets and the correlation between backbone and side chain dihedral angles support the propensity-based mechanism of triple helix stabilization/destabilization induced by hydroxyproline. Furthermore, the analysis of [(Pro-Pro-Gly)10]3 packing, which is governed by electrostatic interactions, suggests that charges may act as locking features in the axial organization of triple helices in the collagen fibrils.
Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3
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Crystal structure of the collagen triple helix model [(Pro-Pro-Gly)10]3
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Biomed Res Int (ISSN: 2314-6133, 2314-6141, 2314-6141electronic), 2013; 2013: N/D-N/D.
Impact Factor: 2.13
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Vergara A, Montesarchio D, Russo Krauss I, Paduano L, Merlino A
* Investigating The Ruthenium Metallation Of Proteins: X-Ray Structure And Raman Microspectroscopy Of The Complex Between Rnase A And Aziru (255 views)
Inorg Chem (ISSN: 0020-1669, 1520-510xe, 1520-510xelectronic), 2013; 52(19): 10714-10716.
Impact Factor: 4.794
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Berisio R
* Learning from pathogens: Exploiting host-pathogen liaison for therapeutic development (364 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2012 Dec; 13(8): 697-698.
Impact Factor: 2.326
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Berisio R, Vitagliano L
* Polyproline and triple helix motifs in Host-Pathogen recognition (746 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2012 Dec; 13(8): 855-865.
Impact Factor: 2.326
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Coppola D, Abbruzzetti S, Nicoletti F, Merlino A, Gambacurta A, Giordano D, Howes BD, De Sanctis G, Vitagliano L, Bruno S, di Prisco G, Mazzarella L, Smulevich G, Coletta M, Viappiani C, Vergara A, Verde C
* ATP regulation of the ligand-binding properties in temperate and cold-adapted haemoglobins. X-ray structure and ligand-binding kinetics in the sub-Antarctic fish Eleginops maclovinus (310 views)
Molecular Biosystems (ISSN: 1742-206x), 2012 Oct 30; 8(12): 3295-3304.
Impact Factor: 3.35
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Diana D, Basile A, De Rosa L, Di Stasi R, Auriemma S, Arra C, Pedone C, Turco MC, Fattorusso R, D'Andrea LD
* Beta-Hairpin Peptide That Targets Vascular Endothelial Growth Factor (vegf) Receptors: Design, Nmr Characterization, And Biological Activity (546 views)
Jbc Papers (ISSN: 1083-351x, 0021-9258, 0021-9258linking), 2011 Dec 2; 286(48): 41680-41691.
Impact Factor: 4.773
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Puglisi A, Rizzarelli E, Vecchio G, Iacovino R, Benedetti E, Pedone C, Saviano M
* Crystal And Molecular Structure Of Beta-Cyclodextrins Functionalized With The Anti-Inflammatory Drug Etodolac (400 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1227-1235.
Impact Factor: 2.605
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Berisio R, De Simone A, Ruggiero A, Improta R, Vitagliano L
* Role of side chains in collagen triple helix stabilization and partner recognition (611 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2009 Mar; 15(3): 131-140.
Impact Factor: 1.807
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Ruggiero A, Tizzano B, Pedone E, Pedone C, Wilmanns M, Berisio R
* Crystal Structure of the Resuscitation-Promoting Factor (Delta DUF)RpfB from M. tuberculosis (527 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2009 Jan 9; 385(1): 153-162.
Impact Factor: 3.871
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Vergara A, Castagnolo D, Carotenuto L, Vitagliano L, Berisio R, Sorrentino G, Gonzalez-ramirez L, Garcia-ruiz J, Zagari A
* Phase behavior and crystallogenesis under counter-diffusion conditions of the collagen-model peptide (Pro-Pro-Gly)10 (313 views)
J Cryst Growth (ISSN: 0022-0248), 2009 Jan 1; 311(2): 304-309.
Impact Factor: 1.534
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Verde C, Vergara A, Mazzarella L, Di Prisco G
* The Hemoglobins of Fishes Living at Polar Latitudes - Current Knowledge on Structural Adaptations in a Changing Environment (339 views)
Curr Protein Pept Sci (ISSN: 1389-2037, 1389-2037linking), 2008 Dec; 9(6): 578-590.
Impact Factor: 3.011
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Esposito L, Seydel A, Aiello R, Sorrentino G, Cendron L, Zanotti G, Zagari
* The crystal structure of the superoxide dismutase from Helicobacter pylori reveals a structured C-terminal extension (348 views)
Bba-Gen Subjects (ISSN: 1570-9639, 0006-3002, 0925-4439), 2008 Nov; 1784(11): 1601-1606.
Impact Factor: 2.233
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De Simone A, Vitagliano L, Berisio R
* Role of hydration in collagen triple helix stabilization (362 views)
Biochem Biophys Res Commun (ISSN: 0006-291x), 2008 Jul 18; 372(1): 121-125.
Impact Factor: 2.648
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Improta R, Berisio R, Vitagliano L
* Contribution of dipole-dipole interactions to the stability of the collagen triple helix (386 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2008 May; 17(5): 955-961.
Impact Factor: 3.115
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D'Ambrosio K, Masereel B, Thiry A, Scozzafava A, Supuran CT, De Simone G
* Carbonic anhydrase inhibitors: Binding of indanesulfonamides to the human isoform II (345 views)
Chemmedchem (ISSN: 1860-7179, 1860-7187, 1860-7187electronic), 2008 Mar; 3(3): 473-477.
Impact Factor: 3.15
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Salvatore A, Cigliano L, Bucci EM, Corpillo D, Velasco S, Carlucci A, Pedone C, Abrescia P
* Haptoglobin binding to apolipoprotein A-I prevents damage from hydroxyl radicals on its stimulatory activity of the enzyme lecithin-cholesterol acyl-transferase (374 views)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2007 Oct 2; 46(39): 11158-11168.
Impact Factor: 3.368
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Merlino A, Sica F, Mazzarella L
* Approximate values for force constant and wave number associated with a low-frequency concerted motion in proteins can be evaluated by a comparison of X-ray structures (201 views)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2007 May 17; 111(19): 5483-5486.
Impact Factor: 4.086
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Pailot A, D'Ambrosio K, Corbier C, Talfournier F, Branlant G
* Invariant Thr(244) is essential for the efficient acylation step of the non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans (315 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2006 Dec 15; 400: 521-530.
Impact Factor: 4.1
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Merlino A, Mazzarella L, Carannante A, Di Fiore A, Di Donato A, Notomista E, Sica F
* The importance of dynamic effects on the enzyme activity: X-ray structure and molecular dynamics of onconase mutants (431 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 May 6; 280(18): 17953-17960.
Impact Factor: 5.854
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Berisio R, Granata V, Vitagliano L, Zagari A
* Imino acids and collagen triple helix stability: Characterization of collagen-like polypeptides containing Hyp-Hyp-Gly sequence repeats (411 views)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2004 Sep 22; 126(37): 11402-11403.
Impact Factor: 6.903
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Berisio R, Granata V, Vitagliano L, Zagari A
* Characterization of Collagen-Like Heterotrimers: Implications for Triple-Helix Stability (369 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2004 Apr 15; 73(6): 682-688.
Impact Factor: 2.863
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Berisio R, Vitagliano L, Vergara A, Sorrentino G, Mazzarella L, Zagari A
* Crystallization of the collagen-like polypeptide (PPG)10 aboard the International Space Station. 2. Comparison of crystal quality by X-ray diffraction (491 views)
Acta Crystallogr D Biol Crystallogr (ISSN: 0907-4449, 0907-4449linking), 2002 Oct; 58(10II): 1695-1699.
Impact Factor: 1.76
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Riccio A, Vitagliano L, Di Prisco G, Zagari A, Mazzarella L
* The crystal structure of a tetrameric hemoglobin in a partial hemichrome state (415 views)
P Natl Acad Sci Usa (ISSN: 0027-8424, 1091-6490, 0027-8424print), 2002 Jul 23; 99(15): 9801-9806.
Impact Factor: 10.7
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Berisio R, Vitagliano L, Mazzarella L, Zagari A
* Recent progress on collagen triple helix structure, stability and assembly (327 views)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2002 Apr; 9(2): 107-116.
Impact Factor: 0.622
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Benzi C, Improta R, Scalmani G, Barone V
* Quantum mechanical study of the conformational behavior of proline and 4R-hydroxyproline dipeptide analogues in vacuum and in aqueous solution (285 views)
J Comput Chem (ISSN: 0192-8651, 1096-987xelectronic), 2002 Feb; 23(3): 341-350.
Impact Factor: 2.931
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Vitagliano L, Berisio R, Mastrangelo A, Mazzarella L, Zagari A
* Preferred proline puckerings in cis and trans peptide groups: Implications for collagen stability (600 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2001 Dec; 10(12): 2627-2632.
Impact Factor: 3.472
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Menchise V, Corbier C, Didierjean C, Saviano M, Benedetti E, Jacquot JP, Aubry A
* Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism (378 views)
Biochem J (ISSN: 0264-6021, 1470-8728electronic, 0264-6021linking), 2001 Oct 1; 359(1): 65-75.
Impact Factor: 4.326
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Vitagliano L, Berisio R, Mazzarella L, Zagari A
* Structural bases of collagen stabilization induced by proline hydroxylation (653 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2001 Apr 15; 58(5): 459-464.
Impact Factor: 1.845
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Romanelli A, Garella I, Menchise V, Iacovino R, Saviano M, Montesarchio D, Didierjean C, Lello PD, Rossi F, Benedetti E
* Crystal-state conformation of Cα, α-dialkylated peptides containing chiral β-homo-residues (454 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2001; 7(1): 15-26.
Impact Factor: 1.451
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Vitagliano L, Merlino A, Zagari A, Mazzarella L
Productive and nonproductive binding to ribonuclease A: X-ray structure of two complexes with uridylyl(2 ', 5 ')guanosine (367 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2000 Jun; 9(6): 1217-1225.
Impact Factor: 3.869
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Berisio R, Vitagliano L, Mazzarella L, Zagari A
Crystal Structure Of A Collagen-Like Polypeptide With Repeating Sequence Pro-Hyp-Gly At 1. 4 Ang Resolution: Implications For Collagen Hydration (411 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2000; 56(1): 8-13.
Impact Factor: 2.405
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Mazzarella L, D'Avino R, Di Prisco G, Savino C, Vitagliano L, Moody P, Zagari A
Crystal structure of Trematomus newnesi haemoglobin re-opens the Root effect question (340 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1999 Apr 16; 287(5): 897-906.
Impact Factor: 5.501
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Vitagliano L, Adinolfi S, Riccio A, Sica F, Zagari A, Mazzarella L
Binding of a substrate analog to a domain swapping protein: X-ray structure of the complex of bovine seminal ribonuclease with uridylyl(2 ', 5 ')adenosine (335 views)
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 1998 Sep; 7(8): 1691-1699.
Impact Factor: 4.44
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Kramer RZ, Vitagliano L, Bella J, Berisio R, Mazzarella L, Brodsky B, Zagari A, Berman HM
X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly) (409 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 1998 Jul 24; 280(4): 623-638.
Impact Factor: 5.803
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Pavone V, Rossi F, Pucci P, Andini S, Ferrara L, Di Blasio B, Pedone C
Studies on gliadin related peptides. I. Synthesis, purification and 1H n. m. r. characterization of the pentapeptide H-Tyr-(Gln)3-Pro-OH (1017 views)
Int J Pept Protein Res (ISSN: 0367-8377, 0367-8377print), 1983 Oct; 22(4): 482-488.
Impact Factor: 1.255
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48 Records (48 excluding Abstracts).
Total impact factor: 185.733 (185.733 excluding Abstracts).
Total 5 year impact factor: 205.035 (205.035 excluding Abstracts).
Total impact factor: 185.733 (185.733 excluding Abstracts).
Total 5 year impact factor: 205.035 (205.035 excluding Abstracts).
402 views. Last view on Thursday 22 September 2022, 4:43:24
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