1xow

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[[Image:1xow.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_1xow| PDB=1xow | SCENE= }}
{{STRUCTURE_1xow| PDB=1xow | SCENE= }}
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'''Crystal structure of the human androgen receptor ligand binding domain bound with an androgen receptor NH2-terminal peptide, AR20-30, and R1881'''
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===Crystal structure of the human androgen receptor ligand binding domain bound with an androgen receptor NH2-terminal peptide, AR20-30, and R1881===
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==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.
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The line below this paragraph, {{ABSTRACT_PUBMED_15525515}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 15525515 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15525515}}
==About this Structure==
==About this Structure==
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[[Category: Human androgen receptor ligand binding domain]]
[[Category: Human androgen receptor ligand binding domain]]
[[Category: R1881]]
[[Category: R1881]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:18:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:15:16 2008''

Revision as of 04:15, 29 July 2008

Image:1xow.png

Template:STRUCTURE 1xow

Crystal structure of the human androgen receptor ligand binding domain bound with an androgen receptor NH2-terminal peptide, AR20-30, and R1881

Template:ABSTRACT PUBMED 15525515

About this Structure

1XOW is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

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