1bhl: Difference between revisions

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{{STRUCTURE_1bhl|  PDB=1bhl  |  SCENE=  }}  
{{STRUCTURE_1bhl|  PDB=1bhl  |  SCENE=  }}  


'''CACODYLATED CATALYTIC DOMAIN OF HIV-1 INTEGRASE'''
===CACODYLATED CATALYTIC DOMAIN OF HIV-1 INTEGRASE===




==Overview==
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Human immunodeficiency virus (HIV) integrase is the enzyme responsible for insertion of a DNA copy of the viral genome into host DNA, an essential step in the replication cycle of HIV. HIV-1 integrase comprises three functional and structural domains: an N-terminal zinc-binding domain, a catalytic core domain and a C-terminal DNA-binding domain. The catalytic core domain with the F185H mutation has been crystallized without sodium cacodylate in a new crystal form, free and complexed with the catalytic metal Mg2+. The structures have been determined and refined to about 2.2 A. Unlike the previously reported structures, the three active-site carboxylate residues (D,D-35-E motif) are well ordered and both aspartate residues delineate a proper metal-binding site. Comparison of the active binding site of this domain with that of other members from the polynucleotidyl transferases superfamily shows a high level of similarity, providing a confident template for the design of antiviral agents.
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==About this Structure==
==About this Structure==
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[[Category: Polynucleotidyl transferase]]
[[Category: Polynucleotidyl transferase]]
[[Category: Polyprotein]]
[[Category: Polyprotein]]
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Revision as of 19:10, 30 June 2008

File:1bhl.png

Template:STRUCTURE 1bhl

CACODYLATED CATALYTIC DOMAIN OF HIV-1 INTEGRASECACODYLATED CATALYTIC DOMAIN OF HIV-1 INTEGRASE

Template:ABSTRACT PUBMED 9735293

About this StructureAbout this Structure

1BHL is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of the catalytic domain of HIV-1 integrase free and complexed with its metal cofactor: high level of similarity of the active site with other viral integrases., Maignan S, Guilloteau JP, Zhou-Liu Q, Clement-Mella C, Mikol V, J Mol Biol. 1998 Sep 18;282(2):359-68. PMID:9735293

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