Structural basis for the activation and ligand recognition of the human oxytocin receptor.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
18 07 2022
18 07 2022
Historique:
received:
25
02
2022
accepted:
10
06
2022
entrez:
19
7
2022
pubmed:
20
7
2022
medline:
22
7
2022
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 35851571
doi: 10.1038/s41467-022-31325-0
pii: 10.1038/s41467-022-31325-0
pmc: PMC9293896
doi:
Substances chimiques
Ligands
0
Receptors, Oxytocin
0
Receptors, Vasopressin
0
Oxytocin
50-56-6
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4153Informations de copyright
© 2022. The Author(s).
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