Identification of the amino acid residues involved in selective agonist binding in the first extracellular loop of the delta- and mu-opioid receptors.

Abstract:

:Effects of amino acid substitutions in the first extracellular loop region of the delta- and mu-opioid receptors were examined. Substitution of lysine-108 of the delta-receptor (delta K108) with asparagine improved affinity to [D-Ala2,MePhe4,Gly-ol5]enk ephalin (DAGO), a mu-selective peptide agonist, to be comparable with that of the mu-receptor. On the other hand, replacement of mN127 with lysine decreased the affinity to DAGO by approximately 15-fold. These results suggest that dK108 and mN127, which correspond to each other in the aligned amino acid sequences, mainly determine the difference in DAGO binding affinity between the delta- and mu-receptors.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Fukuda K,Terasako K,Kato S,Mori K

doi

10.1016/0014-5793(95)01034-c

subject

Has Abstract

pub_date

1995-10-09 00:00:00

pages

177-81

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(95)01034-C

journal_volume

373

pub_type

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