7XKD

Cryo-EM structure of DHEA-ADGRG2-BT-Gs complex

7XKD の概要

• エントリーDOI: 10.2210/pdb7xkd/pdb
• EMDBエントリー: 33248
• 分子名称: Guanine nucleotide-binding protein G(s) subunit alpha isoforms short, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, ... (7 entities in total)
• 機能のキーワード: membrane protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 140384.10

構造登録者

Guo, S.C.,Xiao, P.,Lin, H.,Sun, J.P.,Yu, X. (登録日: 2022-04-19, 公開日: 2022-08-10, 最終更新日: 2025-07-02)

主引用文献

Lin, H.,Xiao, P.,Bu, R.Q.,Guo, S.,Yang, Z.,Yuan, D.,Zhu, Z.L.,Zhang, C.X.,He, Q.T.,Zhang, C.,Ping, Y.Q.,Zhao, R.J.,Ma, C.S.,Liu, C.H.,Zhang, X.N.,Jiang, D.,Huang, S.,Xi, Y.T.,Zhang, D.L.,Xue, C.Y.,Yang, B.S.,Li, J.Y.,Lin, H.C.,Zeng, X.H.,Zhao, H.,Xu, W.M.,Yi, F.,Liu, Z.,Sun, J.P.,Yu, X.
Structures of the ADGRG2-G s complex in apo and ligand-bound forms.
Nat.Chem.Biol., 18:1196-1203, 2022

PubMed Abstract: Adhesion G protein-coupled receptors are elusive in terms of their structural information and ligands. Here, we solved the cryogenic-electron microscopy (cryo-EM) structure of apo-ADGRG2, an essential membrane receptor for maintaining male fertility, in complex with a G trimer. Whereas the formations of two kinks were determinants of the active state, identification of a potential ligand-binding pocket in ADGRG2 facilitated the screening and identification of dehydroepiandrosterone (DHEA), dehydroepiandrosterone sulfate and deoxycorticosterone as potential ligands of ADGRG2. The cryo-EM structures of DHEA-ADGRG2-G provided interaction details for DHEA within the seven transmembrane domains of ADGRG2. Collectively, our data provide a structural basis for the activation and signaling of ADGRG2, as well as characterization of steroid hormones as ADGRG2 ligands, which might be used as useful tools for further functional studies of the orphan ADGRG2.

PubMed: 35982227
DOI: 10.1038/s41589-022-01084-6

実験手法

ELECTRON MICROSCOPY (2.4 Å)