Fig. 2: Thiamine recognition and transport in SLC19A3.
From: Substrate transport and drug interaction of human thiamine transporters SLC19A2/A3
a Cut-open view of apo SLC19A3 outward-open structure, rendered by electrostatic potential (red to blue, −50 kT/e to +50 kT/e). b Cartoon representation of the SLC19A3 outward-open structure, with N- and C-terminal domains (NTD and CTD) colored blue and yellow, respectively. c Thiamine binding pocket of SLC19A3 in the outward-open conformation. d Detailed interactions between thiamine and SLC19A3 in the outward-open conformation. e Thiamine binding site of SLC19A3 in the inward-open conformation. f Detailed interactions between thiamine and SLC19A3 in the inward-open conformation. g [3H] thiamine uptake activity of SLC19A3 mutants in stably transfected HEK 293 T cells. Data were normalized to WT and are presented as mean ± SEM of n = 3 biologically independent experiments. Statistical analysis was performed using two-tailed unpaired Student’s-tests. ****P ≤ 0.0001; EV, empty vector; WT, SLC19A3 wild type; hydrophobic cage, L35A/I36A/T93A/W94A/L97A/V109A.
