Fig. 4: ATD dimer motion across activation states. | Nature Communications

Fig. 4: ATD dimer motion across activation states.

From: Conformational rearrangement of the NMDA receptor amino-terminal domain during activation and allosteric modulation

Fig. 4

a Glycine permits a different glutamate conformational pathway of activation. In all, 100 µM glycine alone (GluN1-closedgly/GluN2B-openempty, red) evokes no detectable FRET change (same as GluN1-openCGP/GluN2B-openempty, blue). In all, 100 µM glycine + 1 mM glutamate (GluN1-closedgly/GluN2B-closedglu, black) increases FRET compared to 1 mM glutamate alone (GluN1-openCGP/GluN2B-closedglu, green). Each histogram n = 5 movies, SEM error bars. b GluN2-competitive antagonist D-APV mimics an early stage of activation. GluN1-competitive antagonist DCKA increases ATD separation induced by D-APV indicating positive cooperativity between the GluN1 and GluN2B subunits. D-APV allows glycine to induce partial rotation (pH 8.5). Each histogram n = 5 movies, SEM error bars. c Neither CGP nor DCKA is capable of unlocking GluN1 to allow rotation (pH 8.5). Each histogram n = 5 movies, SEM error bars. d FRET histograms of SNAP_GluN1-1a/GluN2B (n = 5 movies, SEM error bars) versus SNAP_GluN1-1a/GluN2A (n = 5 movies, SEM error bars) receptors, in the presence of 100 µM glycine and 1 mM glutamate. GluN2A containing receptors exceeds the degree of rotation of the GluN2B in the presence of 100 µM glycine and 1 mM glutamate. Ligands were used at the following concentrations: 100 µM Gly, 1 mM Glu, 3 µM CGP, 100 µM DCKA, and 500 µM D-APV.

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