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. 2020 Mar 20;11:1491. doi: 10.1038/s41467-020-15292-y

Fig. 2. MD simulations of the allosteric interaction between SERT S1 and S1 sites.

Fig. 2

In the presence of S1:S-CIT the Thr497 χ1 dihedral is mostly shifted towards gauche−, whereas in the presence of S1:IMI, it is in gauche+, which in turn affects the salt bridge interaction between S2:S-CIT and Glu494. In all panels, the S1:S-CIT conditions are colored in salmon, whereas the S1:IMI conditions are in purple. a A zoomed-out view of the 5I73 structure showing the S1 and S2 sites. b A zoomed-in view of the equilibrated model of WT S1:S-CIT/S2:apo, c S1:S-CIT/S2:S-CIT, d S1:IMI/S2:apo, and e S1:IMI/S2:S-CIT. g Distribution of the Thr497 χ1 rotamer for S1:S-CIT/S2:apo, S1:IMI/S2:apo (dotted lines), and S1:S-CIT/S2:S-CIT and S1:IMI/S2:S-CIT (solid lines) conditions. h Distribution of the Glu494/S2:S-CIT distance (minimum distance between the charged N of S2:S-CIT and the two carboxyl oxygens of Glu494) for S1:S-CIT/S2:S-CIT and S1:IMI/S2:S-CIT conditions. i S2:S-CIT is more stable in the presence of S1:S-CIT (salmon) than in the presence of S1:IMI (purple) measured by pairwise ligand RMSDs (see “Methods”).