7YDP

Cryo-EM structure of CD97/miniGs complex

Summary for 7YDP

• Entry DOI: 10.2210/pdb7ydp/pdb
• EMDB information: 33755
• Descriptor: Adhesion G protein-coupled receptor E5 subunit beta, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, engineered miniGas, ... (5 entities in total)
• Functional Keywords: gpcr-g-protein complex, membrane protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 5
• Total formula weight: 139584.67

Authors

He, Y.,Wang, N. (deposition date: 2022-07-04, release date: 2023-07-12, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (3.1 Å)