1xq3: Difference between revisions

Revision as of 14:24, 29 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:1xq3.png

Template:STRUCTURE 1xq3

Crystal structure of the human androgen receptor ligand binding domain bound with R1881Crystal structure of the human androgen receptor ligand binding domain bound with R1881

Template:ABSTRACT PUBMED 15525515

About this StructureAbout this Structure

1XQ3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for androgen receptor interdomain and coactivator interactions suggests a transition in nuclear receptor activation function dominance., He B, Gampe RT Jr, Kole AJ, Hnat AT, Stanley TB, An G, Stewart EL, Kalman RI, Minges JT, Wilson EM, Mol Cell. 2004 Nov 5;16(3):425-38. PMID:15525515

Page seeded by OCA on Tue Jul 29 14:24:27 2008

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

OCA

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-'''Crystal structure of the human androgen receptor ligand binding domain bound with R1881'''
+===Crystal structure of the human androgen receptor ligand binding domain bound with R1881===
-==Overview==
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-The androgen receptor (AR) is required for male sex development and contributes to prostate cancer cell survival. In contrast to other nuclear receptors that bind the LXXLL motifs of coactivators, the AR ligand binding domain is preferentially engaged in an interdomain interaction with the AR FXXLF motif. Reported here are crystal structures of the ligand-activated AR ligand binding domain with and without bound FXXLF and LXXLL peptides. Key residues that establish motif binding specificity are identified through comparative structure-function and mutagenesis studies. A mechanism in prostate cancer is suggested by a functional AR mutation at a specificity-determining residue that recovers coactivator LXXLL motif binding. An activation function transition hypothesis is proposed in which an evolutionary decline in LXXLL motif binding parallels expansion and functional dominance of the NH(2)-terminal transactivation domain in the steroid receptor subfamily.
+The line below this paragraph, {{ABSTRACT_PUBMED_15525515}}, adds the Publication Abstract to the page
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 [[Category: Human androgen receptor ligand binding domain]]
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