Ligand Discovery for the Alanine-Serine-Cysteine Transporter (ASCT2, SLC1A5) from Homology Modeling and Virtual Screening
Fig 3
Binding sites of ASCT2 and GltPh differ in their shape, size, and polarity.
The final model of ASCT2 (gray) in an occluded conformation is superimposed on the X-ray structure of GltPh (pink). Key residues are displayed as lines, where oxygen and nitrogen atoms are colored in red and blue, respectively; the sodium ions are visualized as purple spheres. The L-aspartate coordinates from the GltPh structure are depicted by green sticks and L-serine coordinates derived from the docking of known ligands against the ASCT2 model are visualized with cyan sticks. (A) Hydrogen bonds between L-aspartate and GltPh are shown in dotted yellow lines and between L-serine and the ASCT2 model in dotted black lines. (B) The surface of the binding pocket is displayed in pink and gray for the template and the model, respectively, to visualize the additional pocket (pocket B) accessible in the model compared to the GltPh structure.