1bbs
From Proteopedia
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| , resolution 2.8Å | |||||||
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| Activity: | Renin, with EC number 3.4.23.15 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-RAY ANALYSES OF PEPTIDE INHIBITOR COMPLEXES DEFINE THE STRUCTURAL BASIS OF SPECIFICITY FOR HUMAN AND MOUSE RENINS
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Hyperproreninemia OMIM:[179820], Renal tubular dysgenesis OMIM:[179820]
About this Structure
1BBS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
X-ray analyses of peptide-inhibitor complexes define the structural basis of specificity for human and mouse renins., Dhanaraj V, Dealwis CG, Frazao C, Badasso M, Sibanda BL, Tickle IJ, Cooper JB, Driessen HP, Newman M, Aguilar C, et al., Nature. 1992 Jun 11;357(6378):466-72. PMID:1608447
Page seeded by OCA on Thu Mar 20 10:08:52 2008
