1BBS

X-RAY ANALYSES OF PEPTIDE INHIBITOR COMPLEXES DEFINE THE STRUCTURAL BASIS OF SPECIFICITY FOR HUMAN AND MOUSE RENINS

Summary for 1BBS

• Entry DOI: 10.2210/pdb1bbs/pdb
• Descriptor: RENIN (1 entity in total)
• Functional Keywords: aspartic proteinase
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P00797
• Total number of polymer chains: 2
• Total formula weight: 74534.02

Authors

Dhanaraj, V.,Blundell, T.L. (deposition date: 1992-05-21, release date: 1994-01-31, Last modification date: 2024-11-06)

Primary citation

Dhanaraj, V.,Dealwis, C.G.,Frazao, C.,Badasso, M.,Sibanda, B.L.,Tickle, I.J.,Cooper, J.B.,Driessen, H.P.,Newman, M.,Aguilar, C.,Wood, S.P.,Blundell, T.L.,Hobart, P.M.,Geoghegan, K.F.,Ammirati, M.J.,Danley, D.E.
X-ray analyses of peptide-inhibitor complexes define the structural basis of specificity for human and mouse renins.
Nature, 357:466-472, 1992

PubMed Abstract: 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.

PubMed: 1608447
DOI: 10.1038/357466a0

Experimental method

X-RAY DIFFRACTION (2.8 Å)