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

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 liga...

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Autores principales: Waltenspühl, Yann, Ehrenmann, Janosch, Vacca, Santiago, Thom, Cristian, Medalia, Ohad, Plückthun, Andreas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9293896/
https://www.ncbi.nlm.nih.gov/pubmed/35851571
http://dx.doi.org/10.1038/s41467-022-31325-0
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author Waltenspühl, Yann
Ehrenmann, Janosch
Vacca, Santiago
Thom, Cristian
Medalia, Ohad
Plückthun, Andreas
author_facet Waltenspühl, Yann
Ehrenmann, Janosch
Vacca, Santiago
Thom, Cristian
Medalia, Ohad
Plückthun, Andreas
author_sort Waltenspühl, Yann
collection PubMed
description 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.
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spelling pubmed-92938962022-07-20 Structural basis for the activation and ligand recognition of the human oxytocin receptor Waltenspühl, Yann Ehrenmann, Janosch Vacca, Santiago Thom, Cristian Medalia, Ohad Plückthun, Andreas Nat Commun Article 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. Nature Publishing Group UK 2022-07-18 /pmc/articles/PMC9293896/ /pubmed/35851571 http://dx.doi.org/10.1038/s41467-022-31325-0 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Waltenspühl, Yann
Ehrenmann, Janosch
Vacca, Santiago
Thom, Cristian
Medalia, Ohad
Plückthun, Andreas
Structural basis for the activation and ligand recognition of the human oxytocin receptor
title Structural basis for the activation and ligand recognition of the human oxytocin receptor
title_full Structural basis for the activation and ligand recognition of the human oxytocin receptor
title_fullStr Structural basis for the activation and ligand recognition of the human oxytocin receptor
title_full_unstemmed Structural basis for the activation and ligand recognition of the human oxytocin receptor
title_short Structural basis for the activation and ligand recognition of the human oxytocin receptor
title_sort structural basis for the activation and ligand recognition of the human oxytocin receptor
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9293896/
https://www.ncbi.nlm.nih.gov/pubmed/35851571
http://dx.doi.org/10.1038/s41467-022-31325-0
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