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7EW1

Cryo-EM structure of siponimod -bound Sphingosine-1-phosphate receptor 5 in complex with Gi protein

Summary for 7EW1
Entry DOI10.2210/pdb7ew1/pdb
EMDB information31344
DescriptorGuanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, Guanine nucleotide-binding protein G(i) subunit alpha-1, ... (6 entities in total)
Functional Keywordshomo sapiens, membrane protein
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains5
Total formula weight159201.60
Authors
Yuan, Y.,Jia, G.W.,Shao, Z.H.,Su, Z.M. (deposition date: 2021-05-24, release date: 2021-09-29, Last modification date: 2024-11-13)
Primary citationYuan, Y.,Jia, G.,Wu, C.,Wang, W.,Cheng, L.,Li, Q.,Li, Z.,Luo, K.,Yang, S.,Yan, W.,Su, Z.,Shao, Z.
Structures of signaling complexes of lipid receptors S1PR1 and S1PR5 reveal mechanisms of activation and drug recognition.
Cell Res., 31:1263-1274, 2021
Cited by
PubMed Abstract: Sphingosine-1-phosphate (S1P) is an important bioactive lipid molecule in cell membrane metabolism and binds to G protein-coupled S1P receptors (S1PRs) to regulate embryonic development, physiological homeostasis, and pathogenic processes in various organs. S1PRs are lipid-sensing receptors and are therapeutic targets for drug development, including potential treatment of COVID-19. Herein, we present five cryo-electron microscopy structures of S1PRs bound to diverse drug agonists and the heterotrimeric Gi protein. Our structural and functional assays demonstrate the different binding modes of chemically distinct agonists of S1PRs, reveal the mechanical switch that activates these receptors, and provide a framework for understanding ligand selectivity and G protein coupling.
PubMed: 34526663
DOI: 10.1038/s41422-021-00566-x
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.4 Å)
Structure validation

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