1bhl: Difference between revisions
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'''CACODYLATED CATALYTIC DOMAIN OF HIV-1 INTEGRASE''' | '''CACODYLATED CATALYTIC DOMAIN OF HIV-1 INTEGRASE''' | ||
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[[Category: Mikol, V.]] | [[Category: Mikol, V.]] | ||
[[Category: Zhou-Liu, Q.]] | [[Category: Zhou-Liu, Q.]] | ||
[[Category: | [[Category: Aid]] | ||
[[Category: | [[Category: Dna integration]] | ||
[[Category: Endonuclease]] | |||
[[Category: | [[Category: Hydrolase]] | ||
[[Category: | [[Category: Polynucleotidyl transferase]] | ||
[[Category: | [[Category: Polyprotein]] | ||
[[Category: | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:31:20 2008'' | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 11:31, 2 May 2008
CACODYLATED CATALYTIC DOMAIN OF HIV-1 INTEGRASE
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. 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 Page seeded by OCA on Fri May 2 11:31:20 2008