2itg
From Proteopedia
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==Overview== | ==Overview== | ||
| - | We solved the structure and traced the complete active site of the, catalytic domain of the human immunodeficiency virus type 1 integrase, (HIV-1 IN) with the F185H mutation. The only previously available crystal, structure, the F185K mutant of this domain, lacks one of the catalytically, important residues, E152, located in a stretch of 12 disordered residues, [Dyda et al. (1994) Science 266, 1981-1986]. It is clear, however, that, the active site of HIV-1 IN observed in either structure cannot correspond, to that of the functional enzyme, since the cluster of three conserved, carboxylic acids does not create a proper metal-binding site. The, conformation of the loop was compared with two different conformations, found in the catalytic domain of the related avian sarcoma virus integrase, ... | + | We solved the structure and traced the complete active site of the, catalytic domain of the human immunodeficiency virus type 1 integrase, (HIV-1 IN) with the F185H mutation. The only previously available crystal, structure, the F185K mutant of this domain, lacks one of the catalytically, important residues, E152, located in a stretch of 12 disordered residues, [Dyda et al. (1994) Science 266, 1981-1986]. It is clear, however, that, the active site of HIV-1 IN observed in either structure cannot correspond, to that of the functional enzyme, since the cluster of three conserved, carboxylic acids does not create a proper metal-binding site. The, conformation of the loop was compared with two different conformations, found in the catalytic domain of the related avian sarcoma virus integrase, [Bujacz et al. (1995) J. Mol. Biol. 253, 333-346]. Flexibility of the, active site region of integrases may be required in order for the enzyme, to assume a functional conformation in the presence of substrate and/or, cofactors. |
==About this Structure== | ==About this Structure== | ||
| - | 2ITG is a | + | 2ITG 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]. Structure known Active Site: ACT. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ITG 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 13:45:37 2007'' |
Revision as of 11:40, 5 November 2007
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CATALYTIC DOMAIN OF HIV-1 INTEGRASE: ORDERED ACTIVE SITE IN THE F185H CONSTRUCT
Overview
We solved the structure and traced the complete active site of the, catalytic domain of the human immunodeficiency virus type 1 integrase, (HIV-1 IN) with the F185H mutation. The only previously available crystal, structure, the F185K mutant of this domain, lacks one of the catalytically, important residues, E152, located in a stretch of 12 disordered residues, [Dyda et al. (1994) Science 266, 1981-1986]. It is clear, however, that, the active site of HIV-1 IN observed in either structure cannot correspond, to that of the functional enzyme, since the cluster of three conserved, carboxylic acids does not create a proper metal-binding site. The, conformation of the loop was compared with two different conformations, found in the catalytic domain of the related avian sarcoma virus integrase, [Bujacz et al. (1995) J. Mol. Biol. 253, 333-346]. Flexibility of the, active site region of integrases may be required in order for the enzyme, to assume a functional conformation in the presence of substrate and/or, cofactors.
About this Structure
2ITG is a Single protein structure of sequence from Human immunodeficiency virus 1. Structure known Active Site: ACT. Full crystallographic information is available from OCA.
Reference
The catalytic domain of human immunodeficiency virus integrase: ordered active site in the F185H mutant., Bujacz G, Alexandratos J, Qing ZL, Clement-Mella C, Wlodawer A, FEBS Lett. 1996 Dec 2;398(2-3):175-8. PMID:8977101
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