1a5x: Difference between revisions

Revision as of 16:12, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1a5x.png

Template:STRUCTURE 1a5x

ASV INTEGRASE CORE DOMAIN WITH HIV-1 INTEGRASE INHIBITOR Y3ASV INTEGRASE CORE DOMAIN WITH HIV-1 INTEGRASE INHIBITOR Y3

Template:ABSTRACT PUBMED 9560188

About this StructureAbout this Structure

1A5X is a Single protein structure of sequence from Rous sarcoma virus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the catalytic domain of avian sarcoma virus integrase with a bound HIV-1 integrase-targeted inhibitor., Lubkowski J, Yang F, Alexandratos J, Wlodawer A, Zhao H, Burke TR Jr, Neamati N, Pommier Y, Merkel G, Skalka AM, Proc Natl Acad Sci U S A. 1998 Apr 28;95(9):4831-6. PMID:9560188

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OCA

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-'''ASV INTEGRASE CORE DOMAIN WITH HIV-1 INTEGRASE INHIBITOR Y3'''
+===ASV INTEGRASE CORE DOMAIN WITH HIV-1 INTEGRASE INHIBITOR Y3===
-==Overview==
+<!--
-The x-ray structures of an inhibitor complex of the catalytic core domain of avian sarcoma virus integrase (ASV IN) were solved at 1.9- to 2.0-A resolution at two pH values, with and without Mn2+ cations. This inhibitor (Y-3), originally identified in a screen for inhibitors of the catalytic activity of HIV type 1 integrase (HIV-1 IN), was found in the present study to be active against ASV IN as well as HIV-1 IN. The Y-3 molecule is located in close proximity to the enzyme active site, interacts with the flexible loop, alters loop conformation, and affects the conformations of active site residues. As crystallized, a Y-3 molecule stacks against its symmetry-related mate. Preincubation of IN with metal cations does not prevent inhibition, and Y-3 binding does not prevent binding of divalent cations to IN. Three compounds chemically related to Y-3 also were investigated, but no binding was observed in the crystals. Our results identify the structural elements of the inhibitor that likely determine its binding properties.
+The line below this paragraph, {{ABSTRACT_PUBMED_9560188}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9560188 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9560188}}
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 [[Category: Hiv-1 integrase inhibitor]]
 [[Category: Hydrolase]]
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