1bi4
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bi4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bi4 OCA], [http://www.ebi.ac.uk/pdbsum/1bi4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bi4 RCSB]</span> | ||
}} | }} | ||
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[[Category: polyprotein]] | [[Category: polyprotein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:01:24 2008'' |
Revision as of 16:01, 30 March 2008
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, resolution 2.50Å | |||||||
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Sites: | |||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CATALYTIC DOMAIN OF HIV-1 INTEGRASE
Overview
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.
About this Structure
1BI4 is a Protein complex structure of sequences from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
Reference
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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