Figure 7
From: Isoform-specific Inhibition of N-methyl-D-aspartate Receptors by Bile Salts
Structural variability and number of hydrogen bonds in the tauro-CDC-GluN2DLBD and tauro-CDC-GluN3BLBD complexes during the MD simulations. (a) Two-dimensional root-mean-square deviation (RMSD) of the atomic positions of tauro-CDC after least squares fitting of the Cα atom coordinates of the GluN2DLDB in all 10 MD simulations. (b) Two-dimensional root-mean-square deviation (RMSD) of the atomic positions of tauro-CDC after least squares fitting of the Cα atom coordinates of the GluN3BLDB in all 10 MD simulations. (c) Number of hydrogen bonds between tauro-CDC and Arg543 in GluN2DLBD over the course of 10 MD simulations. (d) Number of hydrogen bonds between tauro-CDC and Arg538 in GluN3BLBD over the course of 10 MD simulations. (e) Total humber of hydrogen bonds between tauro-CDC and GluN2DLBD over the course of 10 MD simulations. (f) Total number of hydrogen bonds between tauro-CDC and GluN3BLBD over the course of 10 MD simulations. In panels c and e, data for MD simulation S9 is not shown because here tauro-CDC unbinds after 225 ns (c.f. Supplementary Fig. 3b), and the corresponding data was excluded from statistical analysis.
