1E3G

Human Androgen Receptor Ligand Binding in complex with the ligand metribolone (R1881)

Summary for 1E3G

• Entry DOI: 10.2210/pdb1e3g/pdb
• Related: 1A28
• Descriptor: ANDROGEN RECEPTOR, (17BETA)-17-HYDROXY-17-METHYLESTRA-4,9,11-TRIEN-3-ONE (3 entities in total)
• Functional Keywords: androgen receptor, human androgen receptor, ligand binding domain
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 30949.26

Authors

Matias, P.M.,Donner, P.,Coelho, R.,Thomaz, M.,Peixoto, C.,Macedo, S.,Otto, N.,Joschko, S.,Scholz, P.,Wegg, A.,Basler, S.,Schafer, M.,Ruff, M.,Egner, U.,Carrondo, M.A. (deposition date: 2000-06-14, release date: 2001-06-14, Last modification date: 2024-10-23)

Primary citation

Matias, P.M.,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, M.A.
Structural evidence for ligand specificity in the binding domain of the human androgen receptor. Implications for pathogenic gene mutations.
J. Biol. Chem., 275:26164-26171, 2000

PubMed Abstract: 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.

PubMed: 10840043
DOI: 10.1074/jbc.M004571200

Experimental method

X-RAY DIFFRACTION (2.4 Å)