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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Published in | FEBS letters Vol. 362; no. 1; pp. 19 - 23 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Elsevier B.V
27.03.1995
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Subjects | |
Online Access | Get full text |
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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. |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(95)00150-8 |