1bhl: Difference between revisions
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[[Image:1bhl.gif|left|200px]] | [[Image:1bhl.gif|left|200px]] | ||
'''CACODYLATED CATALYTIC DOMAIN OF HIV-1 INTEGRASE''' | {{Structure | ||
|PDB= 1bhl |SIZE=350|CAPTION= <scene name='initialview01'>1bhl</scene>, resolution 2.20Å | |||
|SITE= <scene name='pdbsite=ACT:Active+Site'>ACT</scene> | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/RNA-directed_DNA_polymerase RNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.49 2.7.7.49] | |||
|GENE= | |||
}} | |||
'''CACODYLATED CATALYTIC DOMAIN OF HIV-1 INTEGRASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1BHL is a [ | 1BHL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BHL OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9735293 9735293] | ||
[[Category: Human immunodeficiency virus 1]] | [[Category: Human immunodeficiency virus 1]] | ||
[[Category: RNA-directed DNA polymerase]] | [[Category: RNA-directed DNA polymerase]] | ||
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[[Category: Mikol, V.]] | [[Category: Mikol, V.]] | ||
[[Category: Zhou-Liu, Q.]] | [[Category: Zhou-Liu, Q.]] | ||
[[Category: | [[Category: aid]] | ||
[[Category: dna binding (viral)]] | [[Category: dna binding (viral)]] | ||
[[Category: dna integration]] | [[Category: dna integration]] | ||
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[[Category: polyprotein]] | [[Category: polyprotein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:11:11 2008'' | ||
Revision as of 11:11, 20 March 2008
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| , resolution 2.20Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Activity: | RNA-directed DNA polymerase, with EC number 2.7.7.49 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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