1bl3

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==Overview==
==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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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==
==About this Structure==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Clement-Mella, C.]]
[[Category: Clement-Mella, C.]]
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[[Category: Guilloteau, J.P.]]
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[[Category: Guilloteau, J P.]]
[[Category: Maignan, S.]]
[[Category: Maignan, S.]]
[[Category: Mikol, V.]]
[[Category: Mikol, V.]]
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[[Category: polyprotein]]
[[Category: polyprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:33:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:56:34 2008''

Revision as of 09:56, 21 February 2008


1bl3, resolution 2.00Å

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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

1BL3 is a Single protein structure of sequence from Human immunodeficiency virus 1 with as ligand. Known structural/functional Site: . 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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