X-ray analyses of peptide–inhibitor complexes define the structural basis of specificity for human and mouse renins
| Autor: | Steve P. Wood, Kieran F. Geoghegan, Peter M. Hobart, B. L. Sibanda, M. Badasso, C. G. Dealwis, M.P. Newman, B. A. O’Connor, C. Aguilar, Mark Ammirati, Dennis J. Hoover, Ian J. Tickle, Carlos Frazão, V. Dhanaraj, Dennis E. Danley, Tom L. Blundell, Jon B. Cooper, H.P.C. Driessen |
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| Rok vydání: | 1992 |
| Předmět: |
Chemical Phenomena
Protein Conformation Sequence analysis Stereochemistry Molecular Sequence Data Peptide Substrate Specificity Mice X-Ray Diffraction Aspartic proteinase inhibitor Renin Renin–angiotensin system Animals Humans Protease Inhibitors Amino Acid Sequence Protein secondary structure chemistry.chemical_classification Binding Sites Multidisciplinary Molecular Structure Chemistry Physical Hydrogen bond Peptide inhibitor Hydrogen Bonding Enzyme Biochemistry chemistry Drug Design Crystallization Oligopeptides Protein Binding |
| Zdroj: | Nature. 357:466-472 |
| ISSN: | 1476-4687 0028-0836 |
| Popis: | X-ray analyses have defined the three-dimensional structures of crystals of mouse and human renins complexed with peptide inhibitors at resolutions of 1.9 and 2.8 A, respectively. The exquisite specificity of renin arises partly from ordered loop regions at the periphery of the binding cleft. Although the pattern of main-chain hydrogen bonding in other aspartic proteinase inhibitor complexes is conserved in renins, differences in the positions of secondary structure elements (particularly helices) also lead to improved specificity in renins for angiotensinogen substrates. |
| Databáze: | OpenAIRE |
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