Researchers at the University of Groningen say they have used cryo-electron microscopy to elucidate the structure of the human glutamine transporter ASCT2, which may generate leads for drug development. The results (“ Cryo-EM structure of the human neutral amino acid transporter ASCT2 ”) are published in Nature Structural & Molecular Biology. “ Human ASCT2 belongs to the SLC1 family of secondary transporters and is specific for the transport of small neutral amino acids. ASCT2 is upregulated in cancer cells and serves as the receptor for many retroviruses; hence, it has importance as a potential drug target. Here we used single-particle cryo-EM to determine a structure of the functional and unmodified human ASCT2 at 3.85-Å resolution. ASCT2 forms a homotrimeric complex in which each subunit contains a transport and a scaffold domain. Prominent extracellular extensions on the scaffold domain form the predicted docking site for retroviruses,” write the investigators. “Relative to ...