Cited by 270Receptor Mechanisms and SignalingNeuroendocrine regulation and behaviorNeuropeptides and Animal Physiology

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The Binding Site of Neuropeptide Vasopressin V1a Receptor

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Mouillac, Bernard, Chini, Bice, Balestre, Marie-Noëlle, Elands, Jack, Trumpp-Kallmeyer, Susanne, Hoflack, Jan, Hibert, Marcel, Jard, Serge, Barberis, Claude·1995·Journal of Biological Chemistry

DOI 10.1074/jbc.270.43.25771

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Abstract

To identify receptor functional domains underlying binding of the neurohypophysial hormones vasopressin (AVP) and oxytocin (OT), we have constructed a three-dimensional (3D) model of the V1a vasopressin receptor subtype and docked the endogenous ligand AVP. To verify and to refine the 3D model, residues likely to be involved in agonist binding were selected for site-directed mutagenesis. Our experimental results suggest that AVP, which is characterized by a cyclic structure, could be completely buried into a 15-20-A deep cleft defined by the transmembrane helices of the receptor and interact with amino acids located within this region. Moreover, the AVP-binding site is situated in a position equivalent to that described for the cationic neurotransmitters. Since all mutated residues are highly conserved in AVP and OT receptors, we propose that the same agonist-binding site is shared by all members of this receptor family. In contrast, the affinity for the antagonists tested, including those with a structure closely related to AVP, is not affected by mutations. This indicates a different binding mode for agonists and antagonists in the vasopressin receptor.

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Authors: Mouillac, B., Chini, B., Balestre, M.-N., Elands, J., Trumpp-Kallmeyer, S., Hoflack, J., Hibert, M., Jard, S., & Barberis, C.
Affiliations: Centre National de la Recherche Scientifique (FR)
Corresponding author: Barberis, Claude
ORCID: Mouillac, Bernard
Chini, Bice
Elands, Jack
Hibert, Marcel
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1995-10
Volume: 270
Issue: 43
Pages: 25771-25777
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.270.43.25771
OpenAlex: W2062176518
Cited by: 262
References: 41
Citations by year: 2026: 2 · 2025: 5 · 2024: 1 · 2023: 1 · 2022: 6 · 2021: 5 · 2020: 8 · 2019: 6 · 2018: 2 · 2017: 5 · 2016: 4 · 2015: 2 · 2014: 4 · 2013: 8 · 2012: 8
FWCI: 5.71
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 9169 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: Institut National de la Santé et de la Recherche Médicale
Centre National de la Recherche Scientifique
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Neuroendocrine regulation and behavior
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
Keywords: vasopressin V1a receptor, vasopressin, oxytocin, receptor binding sites, agonist binding, antagonist binding, protein-ligand docking, site-directed mutagenesis, transmembrane helices, cyclic peptide ligands, neurohypophyseal hormones
MeSH terms: Amino Acid Sequence, Animals, Arginine Vasopressin, Binding Sites, Computer Simulation, DNA Mutational Analysis, Models, Molecular, Molecular Sequence Data, Type C Phospholipases, Protein Binding, Protein Conformation, Radioligand Assay, Recombinant Proteins, Structure-Activity Relationship, Signal Transduction, Mutagenesis, Site-Directed, Sequence Homology, Amino Acid, Receptors, Vasopressin, Receptors, Oxytocin, Rats

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The Binding Site of Neuropeptide Vasopressin V1a Receptor

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