1ex4
From Proteopedia
(New page: 200px<br /> <applet load="1ex4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ex4, resolution 2.80Å" /> '''HIV-1 INTEGRASE CAT...) |
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| - | [[Image:1ex4.gif|left|200px]]<br /> | + | [[Image:1ex4.gif|left|200px]]<br /><applet load="1ex4" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ex4" size=" | + | |
caption="1ex4, resolution 2.80Å" /> | caption="1ex4, resolution 2.80Å" /> | ||
'''HIV-1 INTEGRASE CATALYTIC CORE AND C-TERMINAL DOMAIN'''<br /> | '''HIV-1 INTEGRASE CATALYTIC CORE AND C-TERMINAL DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Insolubility of full-length HIV-1 integrase (IN) limited previous | + | 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== | ==About this Structure== | ||
| - | 1EX4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] with CPS as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1EX4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1] with <scene name='pdbligand=CPS:'>CPS</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EX4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Human immunodeficiency virus 1]] | [[Category: Human immunodeficiency virus 1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chen, J | + | [[Category: Chen, J C.H.]] |
| - | [[Category: Finer-Moore, J | + | [[Category: Finer-Moore, J S.]] |
[[Category: Krucinski, J.]] | [[Category: Krucinski, J.]] | ||
| - | [[Category: Leavitt, A | + | [[Category: Leavitt, A D.]] |
| - | [[Category: Miercke, L | + | [[Category: Miercke, L J.W.]] |
| - | [[Category: Stroud, R | + | [[Category: Stroud, R M.]] |
| - | [[Category: Tang, A | + | [[Category: Tang, A H.]] |
[[Category: CPS]] | [[Category: CPS]] | ||
[[Category: cis-proline]] | [[Category: cis-proline]] | ||
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[[Category: sh3-like domain]] | [[Category: sh3-like domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:32:24 2008'' |
Revision as of 10:32, 21 February 2008
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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 with as ligand. 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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