1e3g

From Proteopedia

Revision as of 08:48, 20 March 2008

HUMAN ANDROGEN RECEPTOR LIGAND BINDING IN COMPLEX WITH THE LIGAND METRIBOLONE (R1881)

Overview

The crystal structures of the human androgen receptor (hAR) and human progesterone receptor ligand-binding domains in complex with the same ligand metribolone (R1881) have been determined. Both three-dimensional structures show the typical nuclear receptor fold. The change of two residues in the ligand-binding pocket between the human progesterone receptor and hAR is most likely the source for the specificity of R1881 to the hAR. The structural implications of the 14 known mutations in the ligand-binding pocket of the hAR ligand-binding domains associated with either prostate cancer or the partial or complete androgen receptor insensitivity syndrome were analyzed. The effects of most of these mutants could be explained on the basis of the crystal structure.

Disease

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 Structure

1E3G is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural evidence for ligand specificity in the binding domain of the human androgen receptor. Implications for pathogenic gene mutations., Matias PM, Donner P, Coelho R, Thomaz M, Peixoto C, Macedo S, Otto N, Joschko S, Scholz P, Wegg A, Basler S, Schafer M, Egner U, Carrondo MA, J Biol Chem. 2000 Aug 25;275(34):26164-71. PMID:10840043

Page seeded by OCA on Thu Mar 20 10:48:58 2008