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1exq

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[[Image:1exq.gif|left|200px]]
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{{Structure
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|RELATEDENTRY=[[1ex4|1EX4]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1exq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1exq OCA], [http://www.ebi.ac.uk/pdbsum/1exq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1exq RCSB]</span>
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'''CRYSTAL STRUCTURE OF THE HIV-1 INTEGRASE CATALYTIC CORE DOMAIN'''
'''CRYSTAL STRUCTURE OF THE HIV-1 INTEGRASE CATALYTIC CORE DOMAIN'''
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[[Category: Stroud, R M.]]
[[Category: Stroud, R M.]]
[[Category: Tang, A H.]]
[[Category: Tang, A H.]]
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[[Category: dd35e]]
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[[Category: Dd35e]]
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[[Category: dna-binding protein]]
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[[Category: Dna-binding protein]]
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[[Category: hiv-1 integrase]]
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[[Category: Hiv-1 integrase]]
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[[Category: polynucleotidyl transferase]]
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[[Category: Polynucleotidyl transferase]]
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Revision as of 12:38, 2 May 2008

Template:STRUCTURE 1exq

CRYSTAL STRUCTURE OF THE HIV-1 INTEGRASE CATALYTIC CORE DOMAIN


Overview

Insolubility of full-length HIV-1 integrase (IN) limited previous structure analyses to individual domains. By introducing five point mutations, we engineered a more soluble IN that allowed us to generate multidomain HIV-1 IN crystals. The first multidomain HIV-1 IN structure is reported. It incorporates the catalytic core and C-terminal domains (residues 52-288). The structure resolved to 2.8 A is a Y-shaped dimer. Within the dimer, the catalytic core domains form the only dimer interface, and the C-terminal domains are located 55 A apart. A 26-aa alpha-helix, alpha6, links the C-terminal domain to the catalytic core. A kink in one of the two alpha6 helices occurs near a known proteolytic site, suggesting that it may act as a flexible elbow to reorient the domains during the integration process. Two proteins that bind DNA in a sequence-independent manner are structurally homologous to the HIV-1 IN C-terminal domain, suggesting a similar protein-DNA interaction in which the IN C-terminal domain may serve to bind, bend, and orient viral DNA during integration. A strip of positively charged amino acids contributed by both monomers emerges from each active site of the dimer, suggesting a minimally dimeric platform for binding each viral DNA end. The crystal structure of the isolated catalytic core domain (residues 52-210), independently determined at 1.6-A resolution, is identical to the core domain within the two-domain 52-288 structure.

About this Structure

1EXQ is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

Reference

Crystal structure of the HIV-1 integrase catalytic core and C-terminal domains: a model for viral DNA binding., Chen JC, Krucinski J, Miercke LJ, Finer-Moore JS, Tang AH, Leavitt AD, Stroud RM, Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8233-8. PMID:10890912 Page seeded by OCA on Fri May 2 15:38:51 2008

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