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Data availability
All data produced or analyzed in this study are included in the main text or the supplementary materials. The cryo-EM density maps and atomic coordinates have been deposited in the Electron Microscopy Data Bank (EMDB) and Protein Data Bank (PDB) under accession numbers EMD-31346 and 7EW3 for the S1P–S1PR3 complex; EMD-31345 and 7EW2 for the pFTY720–S1PR1 complex; EMD-31347 and 7EW4 for the CYM-5541–S1PR1 complex.
References
Cartier, A. & Hla, T. Science 366, eaar5551 (2019).
Pan, S. et al. ACS Med. Chem. Lett. 4, 333–337 (2013).
Guerrero, M. et al. Bioorg. Med. Chem. Lett. 23, 6346–6349 (2013).
Yuan, Y. et al. Cell Res. https://doi.org/10.1038/s41422-021-00566-x (2021).
Shao, Z. et al. Nature 540, 602–606 (2016).
Maeda, S. et al. Sci. Adv. 7, eabf5325 (2021).
Jo, E. et al. ACS Chem. Biol. 7, 1975–1983 (2012).
Deng, Q. et al. Mol. Pharmacol. 71, 724–735 (2007).
Venkatakrishnan, A. J. et al. Nature 494, 185–194 (2013).
Kang, Y. et al. Nature 558, 553–558 (2018).
Acknowledgements
Cryo-EM data were collected at West China Cryo-EM Center in Sichuan University and Cryo-EM Center in Southern University of Science and Technology (SUSTech), processed at Duyu High Performance Computing Center in Sichuan University. This work was supported by the Natural Science Foundation of China (3210110109 to W.Y., 3210110086 to L.C., 32070049 to Z.S.); Ministry of Science and Technology of China grant (2019YFA0508800 to Z.S.); Science and Technology department of Sichuan Province (2020YJ0208 to Z.S.).
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W.W. and L.C. designed the expression constructs, purified the S1PR3–Gi–scFV16 complex; H.W. performed signaling assays with the assistance of Y.F.; W.W. and C.Z. prepared the final samples for data collection toward the structures with the assistance of Y.L., Y.F., X.W., H.F. and Y.C.; C.Z. prepared the cryo-EM grids, collected cryo-EM images, and performed map calculations under the supervision of Z.S.; C.Z. and L.C. built and refined the structure models under the supervision of P.F. and S.Y.; W.Y. and Z.S. supervised the overall project, and wrote the manuscript.
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Zhao, C., Cheng, L., Wang, W. et al. Structural insights into sphingosine-1-phosphate recognition and ligand selectivity of S1PR3–Gi signaling complexes. Cell Res 32, 218–221 (2022). https://doi.org/10.1038/s41422-021-00567-w
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DOI: https://doi.org/10.1038/s41422-021-00567-w
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