Abstract
NMDA-type ionotropic glutamate receptors are composed of two glycine-binding GluN1 and two glutamate-binding GluN2 subunits. Simultaneous occupation of all 4 agonist binding domains allows the receptor to undergo all the conformational changes that lead to opening of the ion channel. Agonist-induced conformational changes in turn alter agonist affinity. Thus, the efficacy by which agonists induce conformational changes and channel gating influences the apparent affinity. Allosteric modulators influence the agonist-induced conformational changes and can therefore alter agonist binding affinity and efficacy.
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