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

Hitomi Shinoura, Hitoshi Take, Akira Hirasawa, Kazuhide Inoue, Yasuo Ohno, Keitaro Hashimoto, Gozoh Tsujimoto

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)

Abstract

A non-peptide, vasopressin V1a receptor-selective antagonist, OPC-21268, exhibited a markedly higher affinity for the rat V1a receptor (K(i)=380 nM) than for the human V1a receptor (K(i)=140 μM). 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. (C) 2000 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)255-258
Number of pages4
JournalFEBS Letters
Volume466
Issue number2-3
DOIs
Publication statusPublished - Jan 28 2000
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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