A single GluN2 subunit residue controls NMDA receptor channel properties via intersubunit interaction.

ABSTRACT: NMDA receptors (NMDARs) are glutamate-gated ion channels that are present at most excitatory mammalian synapses. The four GluN2 subunits (GluN2A-D) contribute to four diheteromeric NMDAR subtypes that have divergent physiological and pathological roles. Channel properties that are fundamental to NMDAR function vary among subtypes. We investigated the amino acid residues responsible for variations in channel properties by creating and examining NMDARs containing mutant GluN2 subunits. We found that the NMDAR subtype specificity of three crucial channel properties, Mg(2+) block, selective permeability to Ca(2+) and single-channel conductance, were all controlled primarily by the residue at a single GluN2 site in the M3 transmembrane region. Mutant cycle analysis guided by molecular modeling

SUBMITTER: Siegler Retchless B 

PROVIDER: S-EPMC3288527 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature