Journal
NATURE COMMUNICATIONS
Volume 13, Issue 1, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41467-022-31325-0
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Funding
- Schweizerischer Nationalfonds Grant [31003A_182334]
- European Research Council [810057-HighResCells]
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In this study, Waltenspuhl et al. have reported the cryo-EM structure of the active human oxytocin receptor in complex with its cognate ligand oxytocin and a heterotrimeric G protein. This structure provides valuable insights into the mechanism of activation of the oxytocin receptor and its subtype specificity within the oxytocin/vasopressin receptor family.
The small cyclic neuropeptide hormone oxytocin (OT) and its cognate receptor play a central role in the regulation of social behaviour and sexual reproduction. Here we report the single-particle cryo-electron microscopy structure of the active oxytocin receptor (OTR) in complex with its cognate ligand oxytocin. Our structure provides high-resolution insights into the OT binding mode, the OTR activation mechanism as well as the subtype specificity within the oxytocin/vasopressin receptor family. Here, Waltenspuhl et al. report the cryo-EM structure of active human oxytocin receptor in complex with oxytocin and with a heterotrimeric G protein, providing insights into this hormone system critically involved in the regulation of social behaviour and reproduction.
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