Arginine-481 mutation abolishes ligand-binding of the AMPA-selective glutamate receptor channel alpha1-subunit

Brain Res Mol Brain Res. 1997 Jul;47(1-2):339-44. doi: 10.1016/s0169-328x(97)00103-4.


Arginine-481 is located in the putative agonist-binding region preceding the putative transmembrane segment M1 of the alpha1-subunit of the AMPA-selective glutamate receptor (GluR) channel. This amino acid is completely conserved among GluR proteins. A site-directed mutagenesis study using a baculovirus expression system showed that substitution of glutamate, glutamine and lysine for arginine-481 of the recombinant alpha1-subunit protein abolishes binding to [3H]AMPA completely. The present study provides the first direct experimental evidence that the conserved charged arginine-481 residue is essential, directly or indirectly, for the acquisition of ligand-binding activity by the receptor protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arginine / metabolism*
  • Base Sequence
  • Ion Channels / drug effects
  • Mice
  • Molecular Sequence Data
  • Mutation / genetics*
  • Radioligand Assay
  • Receptors, Glutamate / drug effects*
  • Receptors, Glutamate / metabolism
  • alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid / pharmacology*


  • Ion Channels
  • Receptors, Glutamate
  • alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid
  • Arginine