1ex4: Difference between revisions
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'''HIV-1 INTEGRASE CATALYTIC CORE AND C-TERMINAL DOMAIN''' | {{Structure | ||
|PDB= 1ex4 |SIZE=350|CAPTION= <scene name='initialview01'>1ex4</scene>, resolution 2.80Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CPS:3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-PROPANESULFONATE'>CPS</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''HIV-1 INTEGRASE CATALYTIC CORE AND C-TERMINAL DOMAIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1EX4 is a [ | 1EX4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EX4 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10890912 10890912] | ||
[[Category: Human immunodeficiency virus 1]] | [[Category: Human immunodeficiency virus 1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sh3-like domain]] | [[Category: sh3-like domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:01:22 2008'' | ||
Revision as of 12:01, 20 March 2008
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HIV-1 INTEGRASE CATALYTIC CORE AND C-TERMINAL DOMAIN
OverviewOverview
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 StructureAbout this Structure
1EX4 is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
ReferenceReference
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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