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Mutations in a putative agonist binding region of the AMPA‐selective glutamate receptor channel
Author(s) -
Uchino Shigeo,
Sakimura Kenji,
Nagahari Kenji,
Mishina Masayoshi
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81286-u
Subject(s) - ampa receptor , protein subunit , glutamic acid , agonist , glutamate receptor , receptor , mutant , chemistry , amino acid , xenopus , biochemistry , transmembrane domain , microbiology and biotechnology , binding site , biology , gene
The region preceding putative transmembrane segment M1 of the glutamate receptor (GluR) channel is well conserved among subunits and has been proposed to constitute a part of the agonist binding site. The functional significance of this region was examined by introducing point mutations into charged residues of the α1 subunit of the mouse α‐amino‐3‐hydroxy‐5‐methyl‐4‐isoxazole propionic acid (AMPA)selective GluR channel. The dose‐response relationships of the mutant receptors were studied after expression in Xenopus oocytes by injection of the mutant α1 subunit‐specific mRNA together with the wild‐type α2‐subunit‐specific mRNA. Variable changes in the EC??? values for different agonists were found for the replacement of glutamic acid 398 by lysine and for the replacement of lysine 445 by glutamic acid. These residues may be involved in selective interaction of the GluR channel with agonists.