From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1ex4.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1ex4.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1ex4| PDB=1ex4 | SCENE= }} | | {{STRUCTURE_1ex4| PDB=1ex4 | SCENE= }} |
| | | | |
| - | '''HIV-1 INTEGRASE CATALYTIC CORE AND C-TERMINAL DOMAIN'''
| + | ===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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10890912}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10890912 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_10890912}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 32: |
Line 36: |
| | [[Category: Nonspecific dna binding beta sheet]] | | [[Category: Nonspecific dna binding beta sheet]] |
| | [[Category: Sh3-like domain]] | | [[Category: Sh3-like domain]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:37:23 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:09:14 2008'' |
Revision as of 23:09, 30 June 2008
Template:STRUCTURE 1ex4
HIV-1 INTEGRASE CATALYTIC CORE AND C-TERMINAL DOMAIN
Template:ABSTRACT PUBMED 10890912
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
Page seeded by OCA on Tue Jul 1 02:09:14 2008
