1bim

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(New page: 200px<br /> <applet load="1bim" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bim, resolution 2.8&Aring;" /> '''CRYSTALLOGRAPHIC STU...)
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Revision as of 14:03, 12 November 2007

Image:1bim.gif

1bim, resolution 2.8Å

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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

1BIM is a Single protein structure of sequence from Homo sapiens with DMF, PHC, HII and IP4 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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