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

Waltenspuehl, Y.; Ehrenmann, J.; Vacca, S.; Thom, C.; Medalia, O.; Plueckthun, A.

doi:10.1101/2022.02.21.481286

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bioRxiv · 10.1101/2022.02.21.481286

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

Waltenspuehl, Y.·Ehrenmann, J.·Vacca, S.·Thom, C.·Medalia, O.·Plueckthun, A.

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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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Waltenspuehl, Y., Ehrenmann, J., Vacca, S., Thom, C., Medalia, O., Plueckthun, A.. 2022-02-22. Structural basis for the activation and ligand recognition of the human oxytocin receptor. https://doi.org/10.1101/2022.02.21.481286

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