Crystal structure of the human oxytocin receptor
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Abstract
that acts as potent, positive allosteric modulator for agonist binding. Together, these results further our molecular understanding of the oxytocin/vasopressin receptor family and will facilitate structure-guided development of new therapeutics.
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Two conserved residues with negative charges of transmembrane helices I and II of the OXTR were identified.
“In addition, the existence of two conserved residues with negative charges of transmembrane helices I and II of the OXTR were also identified (Waltenspuhl et al., 2020).”
From The oxytocin receptor represents a key hub in the GPCR heteroreceptor network: Potential relevance for brain and behavior (2022) · cites this paper as Waltenspuhl et al., 2020
In the crystal structure, cholesterol was bound in a pocket produced by transmembrane helices IV and V.
“In the crystal structure, it was possible to observe that the cholesterol was bound in a pocket produced by transmembrane helices IV and V (Waltenspuhl et al., 2020).”
From The oxytocin receptor represents a key hub in the GPCR heteroreceptor network: Potential relevance for brain and behavior (2022) · cites this paper as Waltenspuhl et al., 2020
The crystal structure of the human OXTR was established in a complex with the OXTR antagonist retosiban.
“Recently, the crystal structure of the human OXTR was established in a complex with the OXTR antagonist retosiban which is in clinical use for counteraction of labor (Waltenspuhl et al., 2020).”
From The oxytocin receptor represents a key hub in the GPCR heteroreceptor network: Potential relevance for brain and behavior (2022) · cites this paper as Waltenspuhl et al., 2020
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Heterodimer of A2A and oxytocin receptors regulating glutamate release in adult striatal astrocytes
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- Authors
- Waltenspühl, Y., Schöppe, J., Ehrenmann, J., Kummer, L., & Plückthun, A.
- Affiliations
- University of Zurich (CH)
- Novo Nordisk (Denmark) (DK)
- Corresponding author
- Plückthun, Andreas
- Venue
- Science Advances
- Published
- 2020-07-17
- Volume
- 6
- Issue
- 29
- Pages
- eabb5419-eabb5419
- ISSN
- 2375-2548 (ISSN-L)
- PMC
- PMC7439316
- OpenAlex
- W3042352447
- Cited by
- 95
- References
- 59
- Citations by year
- 2026: 9 · 2025: 9 · 2024: 11 · 2023: 15 · 2022: 20 · 2021: 26 · 2020: 5
- FWCI
- 5.35
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Science Advances (publishedVersion, cc-by-nc)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- Zurich Open Repository and Archive (University of Zurich) (acceptedVersion, cc-by-nc)
- DORA PSI (Paul Scherrer Institute) (submittedVersion, cc-by-nc)
- Zurich Open Repository and Archive (University of Zurich)
- Funders
- Swiss National Science Foundation (31003A_153143, 31003A_182334)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Social Sciences › Psychology › Social Psychology › Neuroendocrine regulation and behavior
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- oxytocin receptor, crystal structure, positive allosteric modulators, agonist binding, structure-based drug design
- MeSH terms
- Binding Sites, Humans, Oxytocin, Protein Binding, Receptors, Oxytocin
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