Fig. 2

Effects of GluN2B mutations on glutamate potency. a Primary sequence alignment of human NMDAR subunits showing the locations for the four selected mutations. The mutations are shown in colour in the sequence and on the linear subunit structure (crosses) showing the ATD, CTD (C-terminal domain), S1 and S2 regions, plus the M1-M4 TMD. b–e Glutamate concentration–response curves in the presence of 10 μM glycine and normalised to the maximum peak response evoked by saturating glutamate. Control curves in c–e are taken from b. The glutamate EC₅₀s and Hill slopes (n) are: b GluN1–GluN2B^WT 7.18 ± 0.82 μM, 1.45 ± 0.12; GluN2B^C461F 511.40 ± 55.49 μM, 1.44 ± 0.03 unpaired Student’s t-test p < 0.0001, c GluN2B^P553L 12.67 ± 2.01 μM, 0.89 ± 0.05, p < 0.05, d GluN2B^N615I 9.15 ± 1.23μM, 1.27 ± 0.13, p > 0.05; and e GluN2B^V618G 6.08 ± 1.43 μM, 1.23 ± 0.12, p > 0.05. Inset in c shows glutamate-activated currents (to saturating concentration of glutamate and 10 μM glycine) in HEK293 cells expressing GluN1–GluN2B^WT or GluN1–GluN2B^P553L at −30 mV. The red lines show exponential curve fits