Structural basis for the activation and ligand recognition of the human oxytocin receptor

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.

Automated summary

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.