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7X10

ADGRL3/miniG12 complex

Summary for 7X10
Entry DOI10.2210/pdb7x10/pdb
EMDB information32932
Descriptorengineered G alpha 12 subunit, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, scFv16, ... (5 entities in total)
Functional Keywordsgpcr, membrane protein
Biological sourceHomo sapiens
More
Total number of polymer chains5
Total formula weight284055.71
Authors
He, Y.,Qian, Y. (deposition date: 2022-02-22, release date: 2022-11-09, Last modification date: 2024-10-30)
Primary citationQian, Y.,Ma, Z.,Liu, C.,Li, X.,Zhu, X.,Wang, N.,Xu, Z.,Xia, R.,Liang, J.,Duan, Y.,Yin, H.,Xiong, Y.,Zhang, A.,Guo, C.,Chen, Z.,Huang, Z.,He, Y.
Structural insights into adhesion GPCR ADGRL3 activation and Gq, Gs, Gi, and G12 coupling.
Mol.Cell, 82:4340-4352.e6, 2022
Cited by
PubMed Abstract: Adhesion G-protein-coupled receptors (aGPCRs) play key roles in a diversity of physiologies. A hallmark of aGPCR activation is the removal of the inhibitory GAIN domain and the dipping of the cleaved stalk peptide into the ligand-binding pocket of receptors; however, the detailed mechanism remains obscure. Here, we present cryoelectron microscopy (cryo-EM) structures of ADGRL3 in complex with G, G, G, and G. The structures reveal unique ligand-engaging mode, distinctive activation conformation, and key mechanisms of aGPCR activation. The structures also reveal the uncharted structural information of GPCR/G coupling. A comparison of G, G, G, and G engagements with ADGRL3 reveals the key determinant of G-protein coupling on the far end of αH5 of Gα. A detailed analysis of the engagements allows us to design mutations that specifically enhance one pathway over others. Taken together, our study lays the groundwork for understanding aGPCR activation and G-protein-coupling selectivity.
PubMed: 36309016
DOI: 10.1016/j.molcel.2022.10.009
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.93 Å)
Structure validation

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