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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;

/persons/resource/persons255255

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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Citation

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.


Cite as: https://hdl.handle.net/21.11116/0000-0007-F062-B
Abstract
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.