Fig. 5: pH selectively modulates glutamate-induced dimer separation. | Nature Communications

Fig. 5: pH selectively modulates glutamate-induced dimer separation.

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

Fig. 5

a–d Effect of pH on the smFRET histogram of the SNAP_GluN1-1a/GluN2B receptor in 3 µM CGP (n = 5 movies for pH 6.0, 6.3, 6.7, 8.0, and 8.5, n = 4 movies for pH 7.4, 9.0, SEM error bars) (a), 3 µM CGP + 1 mM glutamate (n = 5 movies for pH 6.0, 6.7, 7.4, 8.5, and 9.0, n = 4 movies for pH 6.3, 8.0, SEM error bars) (c), 100 µM glycine (n = 5 movies for each pH condition, SEM error bars) (b), and 100 µM glycine + 1 mM glutamate (n = 5 movies for pH 6.3, 7.4, and 8.5, n = 4 movies for pH 6.0, 6.7, 8.0, and 9.0, SEM error bars) (d). e Little difference in smFRET histograms between pH 6.0 and 8.0 in 100 µM glycine (both histograms n = 5 movies, SEM error bars), but large difference in 100 µM glycine + 1 mM glutamate (both pH 6.0 and 8.0 histograms n = 4 movies, SEM error bars). pH 6.0 brings receptor fully occupied by glycine and glutamate (100 µM glycine + 1 mM glutamate) into a state indistinguishable from the resting Apo state at pH 8.0 (here represented by glycine-bound state). f Mean maximum FRET histogram values in various ligand combinations across pH.

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