This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1exq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1exq.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1exq.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1exq| PDB=1exq | SCENE= }}
{{STRUCTURE_1exq| PDB=1exq | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE HIV-1 INTEGRASE CATALYTIC CORE DOMAIN'''
+
===CRYSTAL STRUCTURE OF THE HIV-1 INTEGRASE CATALYTIC CORE 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 33: Line 37:
[[Category: Hiv-1 integrase]]
[[Category: Hiv-1 integrase]]
[[Category: Polynucleotidyl transferase]]
[[Category: Polynucleotidyl transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:38:51 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:10:56 2008''

Revision as of 23:10, 30 June 2008

Image:1exq.png

Template:STRUCTURE 1exq

CRYSTAL STRUCTURE OF THE HIV-1 INTEGRASE CATALYTIC CORE DOMAIN

Template:ABSTRACT PUBMED 10890912

About this Structure

1EXQ 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 02:10:56 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1exq"
Personal tools