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

Nat Commun. 2022 Jul 18;13(1):4153. doi: 10.1038/s41467-022-31325-0.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cryoelectron Microscopy
  • Humans
  • Ligands
  • Oxytocin* / metabolism
  • Protein Structural Elements
  • Receptors, Oxytocin* / chemistry
  • Receptors, Oxytocin* / genetics
  • Receptors, Oxytocin* / metabolism
  • Receptors, Vasopressin / chemistry
  • Receptors, Vasopressin / metabolism
  • Structure-Activity Relationship

Substances

  • Ligands
  • Receptors, Oxytocin
  • Receptors, Vasopressin
  • Oxytocin