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

Yann Waltenspühl; Janosch Ehrenmann; Santiago Vacca; Cristian Thom; Ohad Medalia; Andreas Plückthun

doi:10.1038/s41467-022-31325-0

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

Yann Waltenspühl
, Janosch Ehrenmann
, Santiago Vacca
, Cristian Thom
, Ohad Medalia
, Andreas Plückthun

Research output: Contribution to journal › Article › peer-review

28 Scopus citations

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.

Original language	English
Article number	4153
Journal	Nature Communications
Volume	13
Issue number	1
DOIs	https://doi.org/10.1038/s41467-022-31325-0
State	Published - 1 Dec 2022
Externally published	Yes

ASJC Scopus subject areas

General Chemistry
General Biochemistry, Genetics and Molecular Biology
General
General Physics and Astronomy

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AU - Medalia, Ohad

AU - Plückthun, Andreas

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

Abstract

ASJC Scopus subject areas

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