1E3G

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

1E3G の概要

• エントリーDOI: 10.2210/pdb1e3g/pdb
• 関連するPDBエントリー: 1A28
• 分子名称: ANDROGEN RECEPTOR, (17BETA)-17-HYDROXY-17-METHYLESTRA-4,9,11-TRIEN-3-ONE (3 entities in total)
• 機能のキーワード: androgen receptor, human androgen receptor, ligand binding domain
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30949.26

構造登録者

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. (登録日: 2000-06-14, 公開日: 2001-06-14, 最終更新日: 2024-10-23)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)