1vsk: Difference between revisions

Revision as of 14:13, 27 July 2008

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File:1vsk.png

Template:STRUCTURE 1vsk

ASV INTEGRASE CORE DOMAIN D64N MUTATION IN CITRATE BUFFER PH 6.0ASV INTEGRASE CORE DOMAIN D64N MUTATION IN CITRATE BUFFER PH 6.0

Template:ABSTRACT PUBMED 9830010

About this StructureAbout this Structure

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

ReferenceReference

Structural basis for inactivating mutations and pH-dependent activity of avian sarcoma virus integrase., Lubkowski J, Yang F, Alexandratos J, Merkel G, Katz RA, Gravuer K, Skalka AM, Wlodawer A, J Biol Chem. 1998 Dec 4;273(49):32685-9. PMID:9830010

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OCA

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-[[Image:1vsk.gif|left|200px]]
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-'''ASV INTEGRASE CORE DOMAIN D64N MUTATION IN CITRATE BUFFER PH 6.0'''
+===ASV INTEGRASE CORE DOMAIN D64N MUTATION IN CITRATE BUFFER PH 6.0===
-==Overview==
+<!--
-Crystallographic studies of the catalytic core domain of avian sarcoma virus integrase (ASV IN) have provided the most detailed picture so far of the active site of this enzyme, which belongs to an important class of targets for designing drugs against AIDS. Recently, crystals of an inactive D64N mutant were obtained under conditions identical to those used for the native enzyme. Data were collected at different pH values and in the presence of divalent cations. Data were also collected at low pH for the crystals of the native ASV IN core domain. In the structures of native ASV IN at pH 6.0 and below, as well as in all structures of the D64N mutants, the side chain of the active site residue Asx-64 (Asx denotes Asn or Asp) is rotated by approximately 150 degrees around the Calpha---Cbeta bond, compared with the structures at higher pH. In the new structures, this residue makes hydrogen bonds with the amide group of Asn-160, and thus, the usual metal-binding site, consisting of Asp-64, Asp-121, and Glu-157, is disrupted. Surprisingly, however, a single Zn2+ can still bind to Asp-121 in the mutant, without restoration of the activity of the enzyme. These structures have elucidated an unexpected mechanism of inactivation of the enzyme by lowering the pH or by mutation, in which a protonated side chain of Asx-64 changes its orientation and interaction partner.
+The line below this paragraph, {{ABSTRACT_PUBMED_9830010}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9830010 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9830010}}
 ==About this Structure==
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 [[Category: Hydrolase]]
 [[Category: Transferase]]
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