7YDH

Cryo EM structure of CD97/miniG13 complex

7YDH の概要

• エントリーDOI: 10.2210/pdb7ydh/pdb
• EMDBエントリー: 33747
• 分子名称: G protein subunit 13 (Gi2-mini-G13 chimera), Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, scFv16, ... (5 entities in total)
• 機能のキーワード: gpcr-g-protein complex, membrane protein
• 由来する生物種: Homo sapiens; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 133175.32

構造登録者

He, Y.,Wang, N. (登録日: 2022-07-04, 公開日: 2023-07-12, 最終更新日: 2024-11-20)

主引用文献

Wang, N.,Qian, Y.,Xia, R.,Zhu, X.,Xiong, Y.,Zhang, A.,Guo, C.,He, Y.
Structural basis of CD97 activation and G-protein coupling.
Cell Chem Biol, 30:1343-1353.e5, 2023

PubMed Abstract: CD97 (ADGRE5) is an adhesion G protein-coupled receptor (aGPCR) which plays crucial roles in immune system and cancer. However, the mechanism of CD97 activation and the determinant of G coupling selectivity remain unknown. Here, we present the cryo-electron microscopy structures of human CD97 in complex with G, G, and G. Our structures reveal the stalk peptide recognition mode of CD97, adding missing information of the current tethered-peptide activation model of aGPCRs. For instance, a revised "FXφφφ" motif and a framework of conserved aromatic residues in the ligand-binding pocket. Importantly, structural comparisons of G, G, and G engagements of CD97 reveal key determinants of G coupling selectivity, where a deep insertion of the α helix 5 and a closer contact with the transmembrane helix 6, 5, and 3 dictate coupling preferences. Taken together, our structural study of CD97 provides a framework for understanding CD97 signaling and the G coupling selectivity.

PubMed: 37673067
DOI: 10.1016/j.chembiol.2023.08.003

実験手法

ELECTRON MICROSCOPY (3.1 Å)