An extracellular residue determines the agonist specificity of V2 vasopressin receptors

FEBS Letters

Gorbulev, Valentin¹  Fahrenholz, Falk¹  Postina, Rolf¹  Ufer, Elke¹ 

[1] Max-Planck-Institute of Biophysics, Kennedyallee 70, 60596 Frankfurt am Main, Germany

关键词: Vasopressin;    Receptor subtype;    Specificity;    Central diabetes insipidus;    AVP;    [8-arginine]vasopressin;    CDI;    central diabetes insipidus;    dDAVP;    1-deamino [8-d-arginine]vasopressin;    DAVP;    [8-d-arginine]vasopressin;    dAVP;    1-deamino [8-arginine] vasopressin;    LVP;    [8-lysine]vasopressin;    OT;    oxytocin;   

DOI  :  10.1016/0014-5793(95)00150-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The specific V₂ agonist 1-deamino [8-d-arginine]-vasopressin (dDAVP), used for treatment of central diabetes insipidus, binds to vasopressin V₂ receptors from human, bovine and rat kidney with an affinity that is similar to that of the natural hormone vasopressin. In contrast, the V₁ receptors and the porcine V₂ receptor do not tolerate a D-arginine in position 8 of vasopressin. By site directed mutagenesis of the cloned bovine and porcine V₂ receptors we identified a residue (Asp-103) in the first extracellular loop of vasopressin receptors which is responsible for high affinity binding of dDAVP.

【 授权许可】

Unknown