1bim
CRYSTALLOGRAPHIC STUDIES ON THE BINDING MODES OF P2-P3 BUTANEDIAMIDE RENIN INHIBITORS
OverviewOverview
The binding modes of three peptidomimetic P2-P3 butanediamide renin inhibitors have been determined by x-ray crystallography. The inhibitors are bound with their backbones in an extended conformation, and their side chains occupying the S5 to S1' pockets. A (2-amino-4-thiazolyl)methyl side chain at the P2 position shows stronger hydrogen-bonding and van der Waals interactions with renin than the His side chain, which is present in the natural substrate. The ACHPA-gamma-lactam transition state analog has similar interactions with renin as the dihydroxyethylene transition state analog.
About this StructureAbout this Structure
1BIM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystallographic studies on the binding modes of P2-P3 butanediamide renin inhibitors., Tong L, Pav S, Lamarre D, Simoneau B, Lavallee P, Jung G, J Biol Chem. 1995 Dec 8;270(49):29520-4. PMID:7493993 Page seeded by OCA on Fri May 2 11:33:38 2008