2ao6

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File:2ao6.gif


2ao6, resolution 1.89Å

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Crystal structure of the human androgen receptor ligand binding domain bound with TIF2(iii) 740-753 peptide and R1881

OverviewOverview

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.

DiseaseDisease

Known diseases associated with this structure: Androgen insensitivity OMIM:[313700], Breast cancer, male, with Reifenstein syndrome OMIM:[313700], Hypospadias, perineal OMIM:[313700], Prostate cancer OMIM:[313700], Prostate cancer, susceptibility to OMIM:[313700], Spinal and bulbar muscular atrophy of Kennedy OMIM:[313700]

About this StructureAbout this Structure

2AO6 is a Protein complex structure of sequences from Homo sapiens with R18 as ligand. This structure superseeds the now removed PDB entry 1XQ2. 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

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