Structural basis for the activation and ligand recognition of the human oxytocin receptor
Y. Waltenspuehl, J. Ehrenmann, S. Vacca, C. Thom, O. Medalia, A. Plueckthun
Abstract
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.
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