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TitleStructural basis for the activation and ligand recognition of the human oxytocin receptor.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 4153, Year 2022
Publish dateJul 18, 2022
AuthorsYann Waltenspühl / Janosch Ehrenmann / Santiago Vacca / Cristian Thom / Ohad Medalia / Andreas Plückthun /
PubMed 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- ...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.
External linksNat Commun / PubMed:35851571 / PubMed Central
MethodsEM (single particle)
Resolution3.25 Å
Structure data

14180

7qvm

EMDB-14180, PDB-7qvm:
Human Oxytocin receptor (OTR) oxytocin Gq chimera (mGoqi) complex
Method: EM (single particle) / Resolution: 3.25 Å

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsSIGNALING PROTEIN / GPCR / OTR / G protein / OT / scFv16 / mGoqi / oxytocin / membrane protein

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