Log in or create a free account to read this content
Gain free access to this article, as well as selected content from this journal and more on nature.com
or
Data availability
The corresponding coordinates and cryo-EM density map have been deposited in the Protein Data Bank (http://www.rcsb.org/pdb) with code 7EXD, and in EMDB (http://www.ebi.ac.uk/pdbe/emdb/) with code EMD-31371.
References
McCorvy, J. D. & Roth, B. L. Pharmacol. Therapeut. 150, 129–142 (2015).
Pytliak, M., Vargova, V., Mechirova, V. & Felsoci, M. Physiol. Res. 60, 15–25 (2011).
Negro, A., Koverech, A. & Martelletti, P. J. Pain Res. 11, 515–526 (2018).
Nelson, D. L. et al. Cephalalgia 30, 1159–1169 (2010).
Weder, C. R. & Schneemann, M. Orphanet J. Rare Dis. 4, 15 (2019).
Clemow, D. B. et al. J. Headache Pain 21, 71 (2020).
Xu, P. et al. Nature 592, 469–473 (2021).
Michino, M. et al. Pharmacol. Rev. 67, 198–213 (2015).
Garcia-Nafria, J., Nehme, R., Edwards, P. C. & Tate, C. G. Nature 558, 620–623 (2018).
Yin, W. et al. Cell Discov. 4, 12 (2018).
Acknowledgements
The cryo-EM data were collected at the Cryo-Electron Microscopy Research Center, Shanghai Institute of Materia Medica, Chinese Academy of Sciences (Shanghai, China). This work was partially supported by the Ministry of Science and Technology of China (2018YFA0507002 to HEX), Strategic Priority Research Program of the Chinese Academy of Sciences (XDB37030103 to HEX), Shanghai Municipal Science and Technology Major Project (2019SHZDZX02 to HEX), the National Natural Science Foundation of China (31770796 to YJ), National Science & Technology Major Project “Key New Drug Creation and Manufacturing Program” (2018ZX09711002-002-002 to YJ).
Author information
Authors and Affiliations
Contributions
SH and PX designed the expression constructs, purified the complexes, prepared samples for negative stain and data collection toward the structures, performed functional assay, prepared the figures and manuscript draft. PX evaluated the specimen by negative-stain EM, screened the cryo-EM conditions, prepared the cryo-EM grids, collected cryo-EM images, built the model, and refined the structures. YT, CY, and YZ participated in the NanoBiT G protein recruitment assays. YJ participated in the supervision of SH, PX, YT, CY and YZ, analyzed the structures, and edited the manuscript. HEX conceived and supervised the project, analyzed the structures, and wrote the manuscript with inputs from all authors.
Corresponding authors
Ethics declarations
Competing interests
The authors declare no competing interests.
Supplementary information
Rights and permissions
About this article
Cite this article
Huang, S., Xu, P., Tan, Y. et al. Structural basis for recognition of anti-migraine drug lasmiditan by the serotonin receptor 5-HT1F–G protein complex. Cell Res 31, 1036–1038 (2021). https://doi.org/10.1038/s41422-021-00527-4
Received:
Accepted:
Published:
Issue date:
DOI: https://doi.org/10.1038/s41422-021-00527-4
This article is cited by
-
G protein-coupled receptors (GPCRs): advances in structures, mechanisms and drug discovery
Signal Transduction and Targeted Therapy (2024)
-
Whether Weather Matters with Migraine
Current Pain and Headache Reports (2024)
-
Structural genomics of the human dopamine receptor system
Cell Research (2023)
-
Structural and functional imaging of brains
Science China Chemistry (2023)
-
Structural insights into the ligand binding and Gi coupling of serotonin receptor 5-HT5A
Cell Discovery (2022)