8H77

Hsp90-AhR-p23-XAP2 complex

8H77 の概要

• エントリーDOI: 10.2210/pdb8h77/pdb
• EMDBエントリー: 34519
• 分子名称: Heat shock protein HSP 90-beta, Prostaglandin E synthase 3, Aryl hydrocarbon receptor, ... (6 entities in total)
• 機能のキーワード: hsp90, ahr, pasb doamin, complex, p23, xap2, cytosolic protein
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 303687.32

構造登録者

Wen, Z.L.,Zhai, Y.J.,Zhu, Y.,Sun, F. (登録日: 2022-10-19, 公開日: 2023-01-04, 最終更新日: 2024-07-03)

主引用文献

Wen, Z.,Zhang, Y.,Zhang, B.,Hang, Y.,Xu, L.,Chen, Y.,Xie, Q.,Zhao, Q.,Zhang, L.,Li, G.,Zhao, B.,Sun, F.,Zhai, Y.,Zhu, Y.
Cryo-EM structure of the cytosolic AhR complex.
Structure, 31:295-, 2023

PubMed Abstract: Aryl hydrocarbon receptor (AhR) is an important ligand-activated transcription factor involved in the regulation of various important physiological functions. Here, we report the cryo-EM structures of the Hsp90-AhR-p23 complex with or without bound XAP2, where the structure of the mouse AhR PAS-B domain is resolved. A highly conserved bridge motif of AhR is responsible for the interaction with the Hsp90 dimeric lumen. The ligand-free AhR PAS-B domain is attached to the Hsp90 dimer and is stabilized in the complex with bound XAP2. In addition, the DE-loop and a group of conserved pocket inner residues in the AhR PAS-B domain are found to be important for ligand binding. These results reveal the structural basis of the biological functions of AhR. Moreover, the protein purification method presented here allows the isolation of stable mouse AhR protein, which could be used to develop high-sensitivity biosensors for environmental pollutant detection.

PubMed: 36649707
DOI: 10.1016/j.str.2022.12.013

実験手法

ELECTRON MICROSCOPY (3.2 Å)