2b4j: Difference between revisions

Revision as of 03:40, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2b4j.png

Template:STRUCTURE 2b4j

Structural basis for the recognition between HIV-1 integrase and LEDGF/p75Structural basis for the recognition between HIV-1 integrase and LEDGF/p75

Template:ABSTRACT PUBMED 16260736

About this StructureAbout this Structure

2B4J is a Protein complex structure of sequences from Homo sapiens and Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75., Cherepanov P, Ambrosio AL, Rahman S, Ellenberger T, Engelman A, Proc Natl Acad Sci U S A. 2005 Nov 29;102(48):17308-13. Epub 2005 Oct 31. PMID:16260736

Page seeded by OCA on Mon Jul 28 03:40:02 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2b4j.gif|left|200px]]
+{{Seed}}
+[[Image:2b4j.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2b4j|  PDB=2b4j  |  SCENE=  }}
-'''Structural basis for the recognition between HIV-1 integrase and LEDGF/p75'''
+===Structural basis for the recognition between HIV-1 integrase and LEDGF/p75===
-==Overview==
+<!--
-Integrase (IN) is an essential retroviral enzyme, and human transcriptional coactivator p75, which is also referred to as lens epithelium-derived growth factor (LEDGF), is the dominant cellular binding partner of HIV-1 IN. Here, we report the crystal structure of the dimeric catalytic core domain of HIV-1 IN complexed to the IN-binding domain of LEDGF. Previously identified LEDGF hotspot residues anchor the protein to both monomers at the IN dimer interface. The principal structural features of IN that are recognized by the host factor are the backbone conformation of residues 168-171 from one monomer and a hydrophobic patch that is primarily comprised of alpha-helices 1 and 3 of the second IN monomer. Inspection of diverse retroviral primary and secondary sequence elements helps to explain the apparent lentiviral tropism of the LEDGF-IN interaction. Because the lethal phenotypes of HIV-1 mutant viruses unable to interact with LEDGF indicate that IN function is highly sensitive to perturbations of the structure around the LEDGF-binding site, we propose that small molecule inhibitors of the protein-protein interaction might similarly disrupt HIV-1 replication.
+The line below this paragraph, {{ABSTRACT_PUBMED_16260736}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16260736 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16260736}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Integration]]
 [[Category: Transcription]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:50:45 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:40:02 2008''