Authors: Yann Waltenspühl, Janosch Ehrenmann, Santiago Vacca, Cristian Thom, Ohad Medalia, Andreas Plückthun
Published: 2022-07-18
DOI: 10.1038/s41467-022-31325-0
Source: Full article
AbstractThe 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.