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FEBS Lett. 2000 Jan 28;466(2-3):255-8.

Key amino acids of vasopressin V1a receptor responsible for the species difference in the affinity of OPC-21268.

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Department of Molecular, Cell Pharmacology, National Children's Medical Research Center, Tokyo, Japan.

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  • FEBS Lett 2000 Jun 2;474(2-3):257.


A non-peptide, vasopressin V1a receptor-selective antagonist, OPC-21268, exhibited a markedly higher affinity for the rat V1a receptor (Ki = 380 nM) than for the human V1a receptor (Ki = 140 microM). To delineate the region responsible for the high affinity binding of OPC-21268 for the rat V1a receptor, we have constructed a series of chimeric human and rat V1a receptors, and examined the chimeric and point-mutated receptors by competitive radioligand binding analysis. The results showed that the transmembrane domain (TMD) VI-VII of the vasopressin V1a receptor, in particular the amino acid residue Ala-342 in TMD VII, is the major component conferring the rat-selective binding of OPC-21268 to the V1a receptor.

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