Bremazocine Recognizes the Difference in Four Amino Acid Residues to Discriminate Between a Nociceptin/Orphanin FQ Receptor and Opioid Receptors

Access this Article

Author(s)

Abstract

We investigated the molecular basis of the discrimination between nociceptin/orphanin FQ receptor (NociR) and opioid receptors (OPRs) by bremazocine, a non-type-selective opioid ligand. Construction of several chimeric receptors between NociR and κ-opioid receptor (KOPR) and mutant NociRs followed by binding experiments with [<SUP>3</SUP>H]bremazocine showed that the mutation of only four amino acid residues of NociR, Ala<SUP>216</SUP>, Val<SUP>279</SUP>, Gln<SUP>280</SUP> and Val<SUP>281</SUP>, to the amino acid residues located at the corresponding position of KOPR, Lys<SUP>227</SUP>, Ile<SUP>290</SUP>, His<SUP>291</SUP> and Ile<SUP>292</SUP>, made it possible for the resultant mutant NociR to bind bremazocine with high affinity. Considering that these four amino acid residues are conserved among μ-, δ- and κ-OPRs, the present result suggests that bremazocine recognizes the difference in these four amino acid residues to discriminate between NociR and OPRs.

Journal

  • The Japanese Journal of Pharmacology

    The Japanese Journal of Pharmacology 77(4), 301-306, 1998-08-01

    The Japanese Pharmacological Society

References:  14

Cited by:  1

Codes

  • NII Article ID (NAID)
    10008193474
  • NII NACSIS-CAT ID (NCID)
    AA00691188
  • Text Lang
    ENG
  • Article Type
    Journal Article
  • ISSN
    00215198
  • NDL Article ID
    4547530
  • NDL Source Classification
    ZS51(科学技術--薬学)
  • NDL Call No.
    Z53-D199
  • Data Source
    CJP  CJPref  NDL  J-STAGE 
Page Top