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. 2021 Feb 18;296:100430. doi: 10.1016/j.jbc.2021.100430

Figure 7.

Figure 7

Dense packing of interfacial residues prevents the binding of AIM-100 to the trimeric interface in the IF TM4-9 mutant. A and B, IF WT human DAT trimer. AIM-100 binds to the trimeric cavity in the IF trimer of WT DAT. For more details see (26). Panel A shows the side view of the trimer, with two AIM-100 binding sites within the trimeric cavity, and the panel B displays the corresponding view from the IC side in space-filling vDW format, showing the AIM-100 bound to the trimeric interface. TM4, TM9, and EL2 loop are colored orange, violet, and green, respectively. C and D, side and IC views of IF TM4-9 mutant trimer. The tight packing of the TM helices 4 and 9 obstruct the central cavity that would otherwise bind AIM-100. DAT, dopamine transporter; IC, intracellular; IF, inward-facing; TM, transmembrane; YFP-HA-DAT, YFP- and HA-epitope tagged DAT.