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-Structure paper
Title | Structural basis for the activation and ligand recognition of the human oxytocin receptor. |
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Journal, issue, pages | Nat Commun, Vol. 13, Issue 1, Page 4153, Year 2022 |
Publish date | Jul 18, 2022 |
Authors | Yann Waltenspühl / Janosch Ehrenmann / Santiago Vacca / Cristian Thom / Ohad Medalia / Andreas Plückthun / |
PubMed 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- ...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 links | Nat Commun / PubMed:35851571 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.25 Å |
Structure data | EMDB-14180, PDB-7qvm: |
Source |
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Keywords | SIGNALING PROTEIN / GPCR / OTR / G protein / OT / scFv16 / mGoqi / oxytocin / membrane protein |