2itg

From Proteopedia

Revision as of 16:10, 5 November 2007

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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