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Data availability
The cryo-EM density maps have been deposited in the Electron Microscopy Data Bank (EMDB) and Protein Data Bank (PDB) under accession numbers EMD-35944 and 8J24 for AA–FFAR2C complex; EMD-35942 and 8J22 for TUG-1375–FFAR2C complex; EMD-35941 and 8J21 for BA–FFAR3C complex; EMD-35940 and 8J20 for VA-AR420626–FFAR3C complex.
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Acknowledgements
We acknowledge support from the National Natural Science Foundation of China (22121003, 21837005, 91953202, 22193023, 32027901 and 31971200), the National Key R&D Program of China (2019YFA0904200, 2019YFA0904101, 2021YFA0910202 and 2022YFA1304701), the Strategic Priority Research Program of Chinese Academy of Sciences (XDB37040203) and the CAS Project for Young Scientists in Basic Research (YSBR-015 and YSBR-072-6).
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J.W. organized the project. J.W., F.L., L.T. and X.L. guided all the structural analyses. J.W. and F.L. designed all the mutants for functional analyses. F.L., Q.G., Z.Z., S.M., S.T. and T.W. developed the FFAR2/3 constructs and optimized protein expression. F.L. performed protein expression. F.L., X.S. and D.G. prepared samples for cryo-EM. F.L. prepared the cryo-EM grids and collected the cryo-EM data. L.T. performed cryo-EM map calculation, model building, and structure refinement. W.T. performed the MD simulations. Z.L., X.Z. and M.Y. performed the functional assays. J.W. and F.L. wrote the manuscript. All the authors have read and commented on the manuscript.
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Li, F., Tai, L., Sun, X. et al. Molecular recognition and activation mechanism of short-chain fatty acid receptors FFAR2/3. Cell Res 34, 323–326 (2024). https://doi.org/10.1038/s41422-023-00914-z
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DOI: https://doi.org/10.1038/s41422-023-00914-z
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