1bim: Difference between revisions

Revision as of 19:13, 30 June 2008

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File:1bim.png

Template:STRUCTURE 1bim

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

Template:ABSTRACT PUBMED 7493993

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

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''CRYSTALLOGRAPHIC STUDIES ON THE BINDING MODES OF P2-P3 BUTANEDIAMIDE RENIN INHIBITORS'''
+===CRYSTALLOGRAPHIC STUDIES ON THE BINDING MODES OF P2-P3 BUTANEDIAMIDE RENIN INHIBITORS===
-==Overview==
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-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_7493993}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7493993 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_7493993}}
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 [[Category: Tong, L.]]
 [[Category: Aspartic proteinase]]
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