X-ray analyses of peptide–inhibitor complexes define the structural basis of specificity for human and mouse renins

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 Å, respectively. The exquisite specificity of renin arises partly from ordered loop regions at the periphery of the binding cleft. Althou...

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Veröffentlicht in:	Nature (London) 1992-06, Vol.357 (6378), p.466-472
Hauptverfasser:	Dhanaraj, V., Dealwis, C. G., Frazao, C., Badasso, M., Sibanda, B. L., Tickle, I. J., Cooper, J. B., Driessen, H. P. C., Newman, M., Aguilar, C., Wood, S. P., Blundell, T. L., Hobart, P. M., Geoghegan, K. F., Ammirati, M. J., Danley, D. E., O'Connor, B. A., Hoover, D. J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Binding Sites Biochemistry Biological and medical sciences Chemical Phenomena Chemistry, Physical complex crystal structure Crystalline structure Crystallization Crystals Drug Design Fundamental and applied biological sciences. Psychology Humanities and Social Sciences Humans Hydrogen Bonding inhibitors man Mice Molecular biophysics Molecular Sequence Data Molecular Structure Molecules multidisciplinary Oligopeptides - chemistry Oligopeptides - metabolism Protease Inhibitors - chemistry Protease Inhibitors - metabolism Protein Binding Protein Conformation Proteinase inhibitors renin Renin - antagonists & inhibitors Renin - chemistry Renin - metabolism Science Science (multidisciplinary) Structure in molecular biology Substrate Specificity X-ray crystallography X-Ray Diffraction
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