The Binding Site of Neuropeptide Vasopressin V1a Receptor
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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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Most critical sites for AVP-V1aR binding are conserved, with one notable exception.
“Like the OTR, most of the critical sites for AVPV1aR binding are conserved (Barberis et al., 1998; Chini et al., 1995; Mouillac et al., 1995; Thibonnier et al., 2000), with one notable exception.”
From Neuropeptide diversity and the regulation of social behavior in New World primates (2016) · cites this paper as Mouillac et al., 1995
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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
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1995-10
- Volume
- 270
- Issue
- 43
- Pages
- 25771-25777
- ISSN
- 0021-9258 (ISSN-L)
- 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
- 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
- Social Sciences › Psychology › Social Psychology › 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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