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Mapping Peptide Antagonist Binding Sites of the Human V1a and V2 Vasopressin Receptors

  • B. Mouillac
  • S. Phalipou
  • N. Cotte
  • M. N. Balestre
  • M. Hibert
  • M. Manning
  • C. Barberis
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 449)

Abstract

For many reasons, the arginine vasopressin (AVP)/oxytocin (OT) receptor family is a particularly suitable system to investigate structure-function relationships among G protein-coupled receptors (GPCR): 1) the Vl a, Vlb, V2 vasopressin receptor subtypes and the OT receptor share a high primary sequence homology. 2) they display a great diversity in their pharmacological and functional properties. 3) a lot of peptide and nonpeptide ligands have been developed and characterized. Constructing three-dimensional (3D) models of these receptors and docking the endogenous ligands vasopressin and oxytocin, already allowed us to localize a transmembrane agonist-binding site (1). Moreover, a residue responsible for the receptor binding selectivity has been found in the first extracellular loop (2). However, these first results towards the identification of AVP/OT receptor binding sites led to very few informations to the definition of antagonist binding domains.

Keywords

Extracellular Loop Vasopressin Receptor Peptide Antagonist Antagonist Binding Vasopressin Antagonist 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

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Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • B. Mouillac
    • 1
  • S. Phalipou
    • 1
  • N. Cotte
    • 1
  • M. N. Balestre
    • 1
  • M. Hibert
    • 2
  • M. Manning
    • 3
  • C. Barberis
    • 1
  1. 1.Unité INSERM 469 CCIPEMontpellier cedex 5France
  2. 2.SynthelaboStrasbourgFrance
  3. 3.Department of Biochemistry and Molecular BiologyMedical College of OhioToledoUSA

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