1bl3
From Proteopedia
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==Overview== | ==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 . | + | 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== | ||
| - | 1BL3 is a | + | 1BL3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: ACT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BL3 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: polyprotein]] | [[Category: polyprotein]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:02:09 2007'' |
Revision as of 12:56, 5 November 2007
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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 MG as ligand. Structure known Active Site: ACT. 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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