1ex4

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ex4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ex4 OCA], [http://www.ebi.ac.uk/pdbsum/1ex4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ex4 RCSB]</span>
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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: CPS]]
 
[[Category: cis-proline]]
[[Category: cis-proline]]
[[Category: nonspecific dna binding beta sheet]]
[[Category: nonspecific dna binding beta sheet]]
[[Category: sh3-like domain]]
[[Category: sh3-like domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:01:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:11:22 2008''

Revision as of 17:11, 30 March 2008


PDB ID 1ex4

Drag the structure with the mouse to rotate
, resolution 2.80Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



HIV-1 INTEGRASE CATALYTIC CORE AND C-TERMINAL 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

1EX4 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

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