Parole chiave: Collagen, Hydration, Hydroxyproline, Supermolecular Structure, Triple Helix, Glycine, Amino Acid Sequence, Article, Crystal Structure, Hydrogen Bond, Molecular Model, Priority Journal, Protein Assembly, Protein Conformation, Protein Structure, X Ray Crystallography, X-Ray, Oligopeptides, Repetitive Sequences, Nucleic Acid,
Affiliazioni:
Department of Chemistry, Rutgers University, 610 Taylor Rd, Piscataway, NJ 08854-8087, United States Waksman Institute, Piscataway, NJ 08855, United States Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, NJ 08855, United States Ctro. di Stud. di Biocristallografia, CNR and Dipartimento di Chimica, Universita' di Napoli, via Mezzocannone 4, 80134 Napoli, Italy Purdue University, Department of Biological Sciences, West Lafayette, IN 47907, United States
Riferimenti:
Acton, S., Resnick, D., Freeman, M., Ekkel, Y., Ashkenas, J., Krieger, M., The collagenous domains of macrophage scavenger receptors and complement component C1q mediate their similar, but not identical, binding specificities for polyanionic ligands (1993) J. Biol. Chem., 268, pp. 3530-353
Bella, J., Berman, H.M., Crystallographic evidence for Cα-H⋯O=C hydrogen bonds in a collagen triple helix (1996) J. Mol. Biol., 264, pp. 734-742
Bella, J., Eaton, M., Brodsky, B., Berman, H.M., Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution (1994) Science, 266, pp. 75-81
Bella, J., Brodsky, B., Berman, H.M., Hydration structure of a collagen peptide (1995) Structure, 3, pp. 893-906
Brünger, A.T., (1992) X-PLOR, Version 3.1, a System for X-ray Crystallography and NMR, , Yale University Press, New Haven, C1
Campbell-Smith, P.J., Arnott, S., LALS: A linked-atom least-squares reciprocal-space refinement system incorporating stereochemical restraints to supplement sparse diffraction data (1978) Acta Crystallog. Sect. A, 34, pp. 3-11
Doi, T., Higashino, K.-I., Kurihara, Y., Wada, Y., Miyazaki, T., Nakamura, H., Uesugi, S., Itakura, H., Charged collagen structure mediates the recognition of negatively charged macromolecules by macrophage scavenger receptors (1993) J. Biol. Chem., 268, pp. 2126-2133
Evans, S.V., SETOR: Hardware lighted three-dimensional solid model representations of macromolecules (1993) J. Mol. Graph., 11, pp. 134-138
Fraser, R.D.B., MacRae, T.P., Suzuki, E., Chain conformation in the collagen molecule (1979) J. Mol. Biol., 129, pp. 463-481
Hendrickson, W.A., Konnert, J.H., PROLSQ (1981) Biomolecular Structure, Conformation, Function and Evolution, pp. 43-57. , (Srinivasan, R., Subramanian, E. & Yathindra, N., eds.), Pergamon Press, Oxford
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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 non-bonded interactions for use in the ECEPP/3 algorithm, with application to proline-containing peptides (1992) J. Phys. Chem., 96, p. 6472
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Campbell-Smith, P. J., Arnott, S., LALS: A linked-atom least-squares reciprocal-space refinement system incorporating stereochemical restraints to supplement sparse diffraction data (1978) Acta Crystallog. Sect. A, 34, pp. 3-11
Evans, S. V., SETOR: Hardware lighted three-dimensional solid model representations of macromolecules (1993) J. Mol. Graph., 11, pp. 134-138
Fair, C. K., (1992) MOLEN: An Interactive Structure Solution Procedure, , Enraf-Nonius, Delft, Netherlands
Fraser, R. D. B., MacRae, T. P., Suzuki, E., Chain conformation in the collagen molecule (1979) J. Mol. Biol., 129, pp. 463-481
Hendrickson, W. A., Konnert, J. H., PROLSQ (1981) Biomolecular Structure, Conformation, Function and Evolution, pp. 43-57. , (Srinivasan, R., Subramanian, E. & Yathindra, N., eds.), Pergamon Press, Oxford
Hoppe, H. -J., Reid, K. B. M., Collectins: Soluble proteins containing collagenous regions and lectin domains and their roles in innate immunity (1994) Protein Sci., 3, pp. 1143-1158
Li, M. -H., Fan, P., Brodsky, B., Baum, J., Two-dimensional NMR assignments and conformation of (Pro-Hyp-Gly) 10 and a designed triple helical peptide (1993) Biochemistry, 32, pp. 7377-7387
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. Symp., 54, pp. 171-200
Momany, F. A., McGuire, R. F., Burgess, A. W., Scheraga, H. A., Energy parameters in polypeptides. VII. Geometric parameters, partial atomic charges, nonbonded interactions, hydrogen bond interactions, and intrinsic torsional potentials for the naturally occuring amino acids (1975) J. Phys. Chem., 79, pp. 2361-2381
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 non-bonded interactions for use in the ECEPP/3 algorithm, with application to proline-containing peptides (1992) J. Phys. Chem., 96, p. 6472
Rich, A., Crick, F. H. C., The molecular structure of collagen (1961) J. Mol. Biol., 3, pp. 483-506
Sack, J. S., CHAIN: A crystallographic modeling program (1988) J. Mol. Graphics., 6, pp. 224-225
The crystal structure of the triple-helical peptide (Pro-Pro-Gly)10 has been re-determined to obtain a more accurate description for this widely studied collagen model and to provide a comparison with the recent high-resolution crystal structure of a collagen-like peptide containing Pro-Hyp-Gly regions. This structure demonstrated that hydroxyproline participates extensively in a repetitive hydrogen-bonded assembly between the peptide and the solvent molecules. Two separate structural studies of the peptide (Pro-Pro-Gly)10 were performed with different crystallization conditions, data collection temperatures, and X-ray sources. The polymer-like structure of one triple-helical repeat of Pro-Pro-Gly has been determined to 2.0 Å resolution in one case and 1.7 Å resolution in the other. The solvent structures of the two peptides were independently determined specifically for validation purposes. The two structures display a reverse chain trace compared with the original structure determination. In comparison with the Hyp-containing peptide, the two Pro-Pro-Gly structures demonstrate very similar molecular conformation and analogous hydration patterns involving carbonyl groups, but have different crystal packing. This difference in crystal packing indicates that the involvement of hydroxyproline in an extended hydration network is critical for the lateral assembly and supermolecular structure of collagen.
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