The role of the hinge loop in domain swapping - The special case of bovine seminal ribonuclease (608 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Apr 8; 280(14): 13771-13778.
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Paper type: Journal Article,
Impact factor: 5.854, 5-year impact factor: 4.863
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-17144424217&partnerID=40&md5=099623efa323e22c4b70c7076043df95
Keywords: Dimers, Dissociation, Phase Equilibria, X Rays, Bovine Seminal Ribonuclease (bs-Rnase), Equilibrium Mixture, Pancreatic Ribonuclease (rnase), Enzymes, Alanine, Proline, Amino Acid Sequence, Amino Acid Substitution, Amino Terminal Sequence, Article, Controlled Study, Disulfide Bond, Hypothesis, Intermethod Comparison, Isomer, Kinetics, Nonhuman, Parameter, Priority Journal, Protein Assembly, Protein Conformation, Protein Domain, Protein Function, Protein Quaternary Structure, Protein Structure, Reduction, Sensitivity Analysis, Sequence Homology, Variance, Waste, X Ray Analysis, Animals, Cattle, Crystallography, X-Ray, Dimerization, Endoribonucleases, Models, Molecular, Mutagenesis, Site-Directed, Peptides, Secondary,
Affiliations:
*** IBB - CNR ***
Dipartimento di Chimica, Univ. Federico II di Napoli, Via Cynthia, 80126, Napoli, Italy
Ist. di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 6, 80134 Napoli, Italy
References:
Not available.
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2005 Apr 8; 280(14): 13771-13778.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.854, 5-year impact factor: 4.863
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-17144424217&partnerID=40&md5=099623efa323e22c4b70c7076043df95
Keywords: Dimers, Dissociation, Phase Equilibria, X Rays, Bovine Seminal Ribonuclease (bs-Rnase), Equilibrium Mixture, Pancreatic Ribonuclease (rnase), Enzymes, Alanine, Proline, Amino Acid Sequence, Amino Acid Substitution, Amino Terminal Sequence, Article, Controlled Study, Disulfide Bond, Hypothesis, Intermethod Comparison, Isomer, Kinetics, Nonhuman, Parameter, Priority Journal, Protein Assembly, Protein Conformation, Protein Domain, Protein Function, Protein Quaternary Structure, Protein Structure, Reduction, Sensitivity Analysis, Sequence Homology, Variance, Waste, X Ray Analysis, Animals, Cattle, Crystallography, X-Ray, Dimerization, Endoribonucleases, Models, Molecular, Mutagenesis, Site-Directed, Peptides, Secondary,
Affiliations:
*** IBB - CNR ***
Dipartimento di Chimica, Univ. Federico II di Napoli, Via Cynthia, 80126, Napoli, Italy
Ist. di Biostrutture e Bioimmagini, CNR, Via Mezzocannone 6, 80134 Napoli, Italy
References:
Not available.
The role of the hinge loop in domain swapping - The special case of bovine seminal ribonuclease
Bovine seminal ribonuclease (BS-RNase) is a covalent homodimeric enzyme homologous to pancreatic ribonuclease (RNase A), endowed with a number of special biological functions. It is isolated as an equilibrium mixture of swapped (MxM) and unswapped (M=M) dimers. The interchanged N termini are hinged on the main bodies through the peptide 16-22, which changes conformation in the two isomers. At variance with other proteins, domain swapping in BS-RNase involves two dimers having a similar and highly constrained quaternary association, mainly dictated by two interchain disulfide bonds. This provides the opportunity to study the intrinsic ability to swap as a function of the hinge sequence, without additional effects arising from dissociation or quaternary structure modifications. Two variants, having Pro(19) or the whole sequence of the hinge replaced by the corresponding residues of RNase A, show equilibrium and kinetic parameters of the swapping similar to those of the parent protein. In comparison, the x-ray structures of MxM indicate, within a substantial constancy of the quaternary association, a greater mobility of the hinge residues. The relative insensitivity of the swapping tendency to the substitutions in the hinge region, and in particular to the replacement of Pro19 by Ala, contrasts with the results obtained for other swapped proteins and can be rationalized in terms of the unique features of the seminal enzyme. Moreover, the results indirectly lend credit to the hypothesis that the major role of Pro19 resides in directing the assembly of the non-covalent dimer, the species produced by selective reduction of the interchain disulfides and considered responsible for the special biological functions of BS-RNase.
Bovine seminal ribonuclease (BS-RNase) is a covalent homodimeric enzyme homologous to pancreatic ribonuclease (RNase A), endowed with a number of special biological functions. It is isolated as an equilibrium mixture of swapped (MxM) and unswapped (M=M) dimers. The interchanged N termini are hinged on the main bodies through the peptide 16-22, which changes conformation in the two isomers. At variance with other proteins, domain swapping in BS-RNase involves two dimers having a similar and highly constrained quaternary association, mainly dictated by two interchain disulfide bonds. This provides the opportunity to study the intrinsic ability to swap as a function of the hinge sequence, without additional effects arising from dissociation or quaternary structure modifications. Two variants, having Pro(19) or the whole sequence of the hinge replaced by the corresponding residues of RNase A, show equilibrium and kinetic parameters of the swapping similar to those of the parent protein. In comparison, the x-ray structures of MxM indicate, within a substantial constancy of the quaternary association, a greater mobility of the hinge residues. The relative insensitivity of the swapping tendency to the substitutions in the hinge region, and in particular to the replacement of Pro19 by Ala, contrasts with the results obtained for other swapped proteins and can be rationalized in terms of the unique features of the seminal enzyme. Moreover, the results indirectly lend credit to the hypothesis that the major role of Pro19 resides in directing the assembly of the non-covalent dimer, the species produced by selective reduction of the interchain disulfides and considered responsible for the special biological functions of BS-RNase.
The role of the hinge loop in domain swapping - The special case of bovine seminal ribonuclease
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The role of the hinge loop in domain swapping - The special case of bovine seminal ribonuclease
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Impact Factor: 2.765
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Ragone R, De Luca S, Tesauro D, Pedone C, Morelli G
Fluorescence studies on the binding between 1-47 fragment of cholecystokinin receptor CCKA-R(1-47) and nonsulfated cholecystokinin octapeptide CCK8 (516 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2000; 56(1): 47-53.
Impact Factor: 2.405
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Gallo P, Rossi F, Saviano M, Pedone C, Colonna G, Ragone R
Specific interaction between bovine cyclophilin A and synthetic analogues of cyclolinopeptide (513 views)
Journal Of Biochemistry (ISSN: 0021-924x), 1998 Nov; 124(5): 880-885.
Impact Factor: 2.189
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Levchenko A, Mehta B, Spengler BA, Narkar A, Fonti R, Biedler JL, Tsuruo T, Larson SM
Measurement of P-glycoprotein expression in multidrug-resistant human neuroblastoma cell lines using self-competitive binding assay (387 views)
Anal Biochem (ISSN: 0003-2697, 1096-0309electronic, 0003-2697linking), 1996 May 1; 236(2): 338-343.
Impact Factor: 2.017
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28 Records (25 excluding Abstracts).
Total impact factor: 88.729 (79.944 excluding Abstracts).
Total 5 year impact factor: 92.479 (83.619 excluding Abstracts).
Total impact factor: 88.729 (79.944 excluding Abstracts).
Total 5 year impact factor: 92.479 (83.619 excluding Abstracts).
608 views. Last view on Sunday 01 December 2024, 6:42:27
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