An extracellular residue determines the agonist specificity of V2 vasopressin 
receptors

Ufer, Elke; Postina, Rolf; Gorbulev, Valentin; Fahrenholz, Falk

doi:10.1016/0014-5793(95)00150-8

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An extracellular residue determines the agonist specificity of V₂ vasopressin receptors

MPS-Authors

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Ufer, Elke
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Postina, Rolf
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Gorbulev, Valentin
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Fahrenholz, Falk
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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引用

Ufer, E., Postina, R., Gorbulev, V., & Fahrenholz, F. (1995). An extracellular residue determines the agonist specificity of V₂ vasopressin receptors. FEBS Letters, 362(1), 19-23. doi:10.1016/0014-5793(95)00150-8.

引用: https://hdl.handle.net/21.11116/0000-0007-F062-B

要旨

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.