2z4j: Difference between revisions

Revision as of 10:32, 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:2z4j.png

Template:STRUCTURE 2z4j

Crystal structure of AR LBD with SHP peptide NR Box 2Crystal structure of AR LBD with SHP peptide NR Box 2

Template:ABSTRACT PUBMED 18007036

About this StructureAbout this Structure

2Z4J is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Interaction between the androgen receptor and a segment of its corepressor SHP., Jouravel N, Sablin E, Arnold LA, Guy RK, Fletterick RJ, Acta Crystallogr D Biol Crystallogr. 2007 Nov;63(Pt 11):1198-200. Epub, 2007 Oct 17. PMID:18007036

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

OCA

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-[[Image:2z4j.jpg|left|200px]]
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-'''Crystal structure of AR LBD with SHP peptide NR Box 2'''
+===Crystal structure of AR LBD with SHP peptide NR Box 2===
-==Overview==
+<!--
-The mechanisms of functional repression of the androgen receptor (AR) are crucial for the regulation of genes involved in physiological development as well as for the progression of prostate cancer. To date, only two in vivo inhibitors of AR-mediated transcription have been identified: DAX-1 and SHP (small heterodimer partner). SHP is a regulatory nuclear receptor (NR) that lacks DNA-binding and activation domains. Using X-ray crystallography, the interaction between peptide segments of the SHP repressor containing LxxLL-like motifs and the ligand-binding domain of AR have been investigated. Under the crystallization conditions used, it was found that of the three NR Boxes present in the SHP protein sequence, only NR Box 2 (LKKIL motif) formed a complex with AR. Determination of the crystal structure revealed that ten amino acids of the SHP peptide (14-mer) are ordered through interactions with AR. Two side chains make unique interactions that were not reported for other AR-peptide complexes. The NR Box 2 of SHP binds to an adaptable hydrophobic groove on the surface of AR in a fashion observed for other NR-LxxLL-like complexes. Comparisons of AR structures bound to coactivator peptides and the SHP peptide revealed structural similarity of their binding sites, suggesting that transcriptional AR activity may be inhibited by SHP by competing with AR coactivators.
+The line below this paragraph, {{ABSTRACT_PUBMED_18007036}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18007036 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18007036}}
 ==About this Structure==
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 [[Category: Shp]]
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-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 19:56:37 2008''
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