1bhl
CACODYLATED CATALYTIC DOMAIN OF HIV-1 INTEGRASE
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OverviewOverview
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 StructureAbout this Structure
1BHL is a Single protein structure of sequence from Human immunodeficiency virus 1. Active as RNA-directed DNA polymerase, with EC number 2.7.7.49 Known structural/functional Site: . 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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