1xow: Difference between revisions
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[[Image:1xow.png|left|200px]] | [[Image:1xow.png|left|200px]] | ||
{{STRUCTURE_1xow| PDB=1xow | SCENE= }} | {{STRUCTURE_1xow| PDB=1xow | SCENE= }} | ||
===Crystal structure of the human androgen receptor ligand binding domain bound with an androgen receptor NH2-terminal peptide, AR20-30, and R1881=== | ===Crystal structure of the human androgen receptor ligand binding domain bound with an androgen receptor NH2-terminal peptide, AR20-30, and R1881=== | ||
{{ABSTRACT_PUBMED_15525515}} | {{ABSTRACT_PUBMED_15525515}} | ||
==About this Structure== | ==About this Structure== | ||
[[1xow]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XOW OCA]. | |||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:015525515</ref><references group="xtra"/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: An, G.]] | [[Category: An, G.]] | ||
[[Category: Gampe, R T.]] | |||
[[Category: He, B.]] | [[Category: He, B.]] | ||
[[Category: Hnat, A T.]] | [[Category: Hnat, A T.]] | ||
[[Category: Kalman, R I.]] | [[Category: Kalman, R I.]] | ||
[[Category: Kole, A J.]] | [[Category: Kole, A J.]] | ||
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[[Category: Human androgen receptor ligand binding domain]] | [[Category: Human androgen receptor ligand binding domain]] | ||
[[Category: R1881]] | [[Category: R1881]] | ||
[[Category: Transcription]] | |||
Revision as of 11:13, 5 January 2013
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 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- He B, Gampe RT Jr, Kole AJ, Hnat AT, Stanley TB, An G, Stewart EL, Kalman RI, Minges JT, Wilson EM. Structural basis for androgen receptor interdomain and coactivator interactions suggests a transition in nuclear receptor activation function dominance. Mol Cell. 2004 Nov 5;16(3):425-38. PMID:15525515 doi:10.1016/j.molcel.2004.09.036
