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8IKJ

Cryo-EM structure of the inactive CD97

Summary for 8IKJ
Entry DOI10.2210/pdb8ikj/pdb
EMDB information35514
DescriptorAdhesion G protein-coupled receptor E5,Soluble cytochrome b562,Adhesion G protein-coupled receptor E5 subunit beta, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
Functional Keywordsadhension gpcr, cd97, inactive, membrane protein
Biological sourceHomo sapiens (human)
More
Total number of polymer chains1
Total formula weight73215.28
Authors
Mao, C.,Zhao, R.,Dong, Y.,Gao, M.,Chen, L.,Zhang, C.,Xiao, P.,Guo, J.,Qin, J.,Shen, D.,Ji, S.,Zang, S.,Zhang, H.,Wang, W.,Shen, Q.,Sun, P.,Zhang, Y. (deposition date: 2023-02-28, release date: 2024-02-14, Last modification date: 2024-10-30)
Primary citationMao, C.,Zhao, R.J.,Dong, Y.J.,Gao, M.,Chen, L.N.,Zhang, C.,Xiao, P.,Guo, J.,Qin, J.,Shen, D.D.,Ji, S.Y.,Zang, S.K.,Zhang, H.,Wang, W.W.,Shen, Q.,Sun, J.P.,Zhang, Y.
Conformational transitions and activation of the adhesion receptor CD97.
Mol.Cell, 84:570-583.e7, 2024
Cited by
PubMed Abstract: Adhesion G protein-coupled receptors (aGPCRs) are evolutionarily ancient receptors involved in a variety of physiological and pathophysiological processes. Modulators of aGPCR, particularly antagonists, hold therapeutic promise for diseases like cancer and immune and neurological disorders. Hindered by the inactive state structural information, our understanding of antagonist development and aGPCR activation faces challenges. Here, we report the cryo-electron microscopy structures of human CD97, a prototypical aGPCR that plays crucial roles in immune system, in its inactive apo and G13-bound fully active states. Compared with other family GPCRs, CD97 adopts a compact inactive conformation with a constrained ligand pocket. Activation induces significant conformational changes for both extracellular and intracellular sides, creating larger cavities for Stachel sequence binding and G13 engagement. Integrated with functional and metadynamics analyses, our study provides significant mechanistic insights into the activation and signaling of aGPCRs, paving the way for future drug discovery efforts.
PubMed: 38215752
DOI: 10.1016/j.molcel.2023.12.020
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.2 Å)
Structure validation

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