1exq: Difference between revisions
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|PDB= 1exq |SIZE=350|CAPTION= <scene name='initialview01'>1exq</scene>, resolution 1.60Å | |PDB= 1exq |SIZE=350|CAPTION= <scene name='initialview01'>1exq</scene>, resolution 1.60Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1ex4|1EX4]] | |||
|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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[[Category: Stroud, R M.]] | [[Category: Stroud, R M.]] | ||
[[Category: Tang, A H.]] | [[Category: Tang, A H.]] | ||
[[Category: dd35e]] | [[Category: dd35e]] | ||
[[Category: dna-binding protein]] | [[Category: dna-binding protein]] | ||
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[[Category: polynucleotidyl transferase]] | [[Category: polynucleotidyl transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:11:44 2008'' | ||
Revision as of 20:11, 30 March 2008
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| , resolution 1.60Å | |||||||
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| Ligands: | , , | ||||||
| Related: | 1EX4
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE HIV-1 INTEGRASE CATALYTIC CORE 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
1EXQ 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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