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N-methyl-D-aspartate receptors (NMDARs) are tetrameric ligand-gated ion channels that are predominantly formed by two GluN1 and two GluN2 subunits.The identity of the GluN2 subunit largely determines the biophysical, pharmacological and signaling properties of NMDAR subtypes.By generating chimeric GluN2 subunits we have identified how the nature of the GluN2 ligand binding domain determines agonist potency at the GluN 1 subunit which offers insights as to why newly described non-competitive antagonists while acting at the GluN1 subunit are selective for GluN2A-containing NMDARs.