2AO6

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

「1XQ2」から置き換えられました

2AO6 の概要

• エントリーDOI: 10.2210/pdb2ao6/pdb
• 関連するPDBエントリー: 1XOW 1XQ3
• 分子名称: androgen receptor, 14-mer fragment of Nuclear receptor coactivator 2, (17BETA)-17-HYDROXY-17-METHYLESTRA-4,9,11-TRIEN-3-ONE, ... (4 entities in total)
• 機能のキーワード: crystal structure; human androgen receptor ligand binding domain; transcriptional intermediary factor 2 740-753; r188, transcription
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus : P10275 Q15596
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32140.68

構造登録者

He, B.,Gampe Jr., R.T.,Kole, A.J.,Hnat, A.T.,Stanley, T.B.,An, G.,Stewart, E.L.,Kalman, R.I.,Minges, J.T.,Wilson, E.M. (登録日: 2005-08-12, 公開日: 2005-08-30, 最終更新日: 2023-08-23)

主引用文献

He, B.,Gampe Jr., R.T.,Kole, A.J.,Hnat, A.T.,Stanley, T.B.,An, G.,Stewart, E.L.,Kalman, R.I.,Minges, J.T.,Wilson, E.M.
Structural basis for androgen receptor interdomain and coactivator interactions suggests a transition in nuclear receptor activation function dominance
Mol.Cell, 16:425-438, 2004

PubMed Abstract: 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.

PubMed: 15525515
DOI: 10.1016/j.molcel.2004.09.036

実験手法

X-RAY DIFFRACTION (1.89 Å)