Insights into the molecular evolution of oxytocin receptor ligand binding
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The design and development of selective ligands for the human OT (oxytocin) and AVP (arginine vasopressin) receptors is a big challenge since the different receptor subtypes and their native peptide ligands display great similarity. Detailed understanding of the mechanism of OT's interaction with its receptor is important and may assist in the ligand- or structure-based design of selective and potent ligands. In the present article, we compared 69 OT- and OT-like receptor sequences with regards to their molecular evolution and diversity, utilized an in silico approach to map the common ligand interaction sites of recently published G-protein-coupled receptor structures to a model of the human OTR (OT receptor) and compared these interacting residues within a selection of different OTR sequences. Our analysis suggests the existence of a binding site for OT peptides within the common transmembrane core region of the receptor, but it appears extremely difficult to identify receptor or ligand residues that could explain the selectivity of OT to its receptors. We remain confident that the presented evolutionary overview and modelling approach will aid interpretation of forthcoming OTR crystal structures.
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A strong coevolutionary relationship between ligand and receptor variation is demonstrated in New World monkeys.
“a strong coevolutionary relationship between ligand and receptor variation is demonstrated”
From Neuropeptide diversity and the regulation of social behavior in New World primates (2016) · cites this paper as Koehbach et al., 2013
A host of invertebrate species express one OT/AVP-like ligand, suggesting a very early evolutionary origin (~600 million years ago) for these signaling molecules.
“A host of invertebrate species express one OT/AVP-like ligand, suggesting a very early evolutionary origin (~600 million years ago; Mya) for these signaling molecules”
From Neuropeptide diversity and the regulation of social behavior in New World primates (2016) · cites this paper as Koehbach et al., 2013
These radical amino acid substitutions lead to altered biochemical properties that could have important implications for receptor binding and subsequent cell signaling.
“leading to altered biochemical properties that could have important implications for receptor binding and subsequent cell signaling (Koehbach et al., 2013)”
From Neuropeptide diversity and the regulation of social behavior in New World primates (2016) · cites this paper as Koehbach et al., 2013
A survey of nucleotide sequences for OT/AVP-like GPCRs among 69 representative invertebrate and vertebrate species revealed considerable ligand-receptor coevolution.
“A survey of nucleotide sequences for OT/AVP-like GPRCs among 69 representative invertebrate and vertebrate species revealed considerable ligand-receptor coevolution (Fig. 3) (Koehbach et al., 2013; Liutkeviciute and Gruber, 2015).”
From Neuropeptide diversity and the regulation of social behavior in New World primates (2016) · cites this paper as Koehbach et al., 2013
A Phe at this position is important for binding to ligands with a Leu or Iso at position 8.
“A Phe at this position is important for binding to ligands with a Leu or Iso at position 8 (Koehbach et al. 2013).”
From Neuropeptide diversity and the regulation of social behavior in New World primates (2016) · cites this paper as Koehbach et al. 2013
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- Authors
- Koehbach, J., Stockner, T., Bergmayr, C., Muttenthaler, M., & Gruber, C. W.
- Affiliations
- Medical University of Vienna (AT)
- Scripps Research Institute (US)
- Corresponding author
- Koehbach, Johannes
- Stockner, Thomas
- Bergmayr, Christian
- Venue
- Biochemical Society Transactions
- Publisher
- Portland Press Ltd.
- Published
- 2013-01-29
- Volume
- 41
- Issue
- 1
- Pages
- 197-204
- ISSN
- 0300-5127 (ISSN-L)
- 1470-8752
- PMC
- PMC3634130
- OpenAlex
- W2157375137
- Cited by
- 61
- References
- 37
- Citations by year
- 2025: 3 · 2024: 6 · 2023: 2 · 2022: 1 · 2021: 3 · 2020: 10 · 2019: 6 · 2018: 6 · 2017: 4 · 2016: 5 · 2015: 4 · 2014: 5 · 2013: 6
- FWCI
- 0.66
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Biochemical Society Transactions (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- 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
- oxytocin receptor, arginine vasopressin receptor, molecular evolution, ligand binding sites, G protein-coupled receptors, ligand-receptor interactions, structure-based ligand design
- MeSH terms
- Amino Acid Sequence, Humans, Ligands, Molecular Sequence Data, Protein Binding, Receptors, Oxytocin, Evolution, Molecular
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