An extracellular residue determines the agonist specificity of V 2 vasopressin receptors

The specific V 2 agonist 1-deamino [8- d-arginine]-vasopressin (dDAVP), used for treatment of central diabetes insipidus, binds to vasopressin V 2 receptors from human, bovine and rat kidney with an affinity that is similar to that of the natural hormone vasopressin. In contrast, the V 1 receptors a...

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Bibliographic Details
Published inFEBS letters Vol. 362; no. 1; pp. 19 - 23
Main Authors Ufer, Elke, Postina, Rolf, Gorbulev, Valentin, Fahrenholz, Falk
Format Journal Article
LanguageEnglish
Published Elsevier B.V 27.03.1995
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Summary:The specific V 2 agonist 1-deamino [8- d-arginine]-vasopressin (dDAVP), used for treatment of central diabetes insipidus, binds to vasopressin V 2 receptors from human, bovine and rat kidney with an affinity that is similar to that of the natural hormone vasopressin. In contrast, the V 1 receptors and the porcine V 2 receptor do not tolerate a D-arginine in position 8 of vasopressin. By site directed mutagenesis of the cloned bovine and porcine V 2 receptors we identified a residue (Asp-103) in the first extracellular loop of vasopressin receptors which is responsible for high affinity binding of dDAVP.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(95)00150-8