7ydp

From Proteopedia

Cryo-EM structure of CD97/miniGs complex

Structural highlights

7ydp is a 5 chain structure with sequence from Homo sapiens and Lama glama. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.1Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

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(13) coupling selectivity remain unknown. Here, we present the cryo-electron microscopy structures of human CD97 in complex with G(13), G(q), and G(s). 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 "FXphiphiphi" motif and a framework of conserved aromatic residues in the ligand-binding pocket. Importantly, structural comparisons of G(13), G(q), and G(s) engagements of CD97 reveal key determinants of G(13) coupling selectivity, where a deep insertion of the alpha 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(13) coupling selectivity.

Structural basis of CD97 activation and G-protein coupling.,Wang N, Qian Y, Xia R, Zhu X, Xiong Y, Zhang A, Guo C, He Y Cell Chem Biol. 2023 Nov 16;30(11):1343-1353.e5. doi: , 10.1016/j.chembiol.2023.08.003. Epub 2023 Sep 5. PMID:37673067^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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. 2023 Nov 16;30(11):1343-1353.e5. PMID:37673067 doi:10.1016/j.chembiol.2023.08.003