1bil

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Image:1bil.jpg

1bil, resolution 2.4Å

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CRYSTALLOGRAPHIC STUDIES ON THE BINDING MODES OF P2-P3 BUTANEDIAMIDE RENIN INHIBITORS

Contents

Overview

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.

Disease

Known diseases associated with this structure: Hyperproreninemia OMIM:[179820], Renal tubular dysgenesis OMIM:[179820]

About this Structure

1BIL is a Single protein structure of sequence from Homo sapiens with , , and as ligands. Full crystallographic information is available from OCA.

Reference

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

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