2itg: Difference between revisions

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[[Image:2itg.gif|left|200px]]
{{Seed}}
[[Image:2itg.png|left|200px]]


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{{STRUCTURE_2itg|  PDB=2itg  |  SCENE=  }}  
{{STRUCTURE_2itg|  PDB=2itg  |  SCENE=  }}  


'''CATALYTIC DOMAIN OF HIV-1 INTEGRASE: ORDERED ACTIVE SITE IN THE F185H CONSTRUCT'''
===CATALYTIC DOMAIN OF HIV-1 INTEGRASE: ORDERED ACTIVE SITE IN THE F185H CONSTRUCT===




==Overview==
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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.
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{{ABSTRACT_PUBMED_8977101}}


==About this Structure==
==About this Structure==
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[[Category: Polynucleotidyl transferase]]
[[Category: Polynucleotidyl transferase]]
[[Category: Polyprotein]]
[[Category: Polyprotein]]
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Revision as of 15:50, 28 July 2008

File:2itg.png

Template:STRUCTURE 2itg

CATALYTIC DOMAIN OF HIV-1 INTEGRASE: ORDERED ACTIVE SITE IN THE F185H CONSTRUCT

Template:ABSTRACT PUBMED 8977101

About this Structure

2ITG is a Single protein structure of sequence from Human immunodeficiency virus 1. 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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