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Cryo-EM structures of the human glutamine transporter SLC1A5 (ASCT2) in the outward-facing conformation
2019
eLife
Alanine-serine-cysteine transporter 2 (ASCT2, SLC1A5) is the primary transporter of glutamine in cancer cells and regulates the mTORC1 signaling pathway. The SLC1A5 function involves finely tuned orchestration of two domain movements that include the substrate-binding transport domain and the scaffold domain. Here, we present cryo-EM structures of human SLC1A5 and its complex with the substrate, L-glutamine in an outward-facing conformation. These structures reveal insights into the
doi:10.7554/elife.48120
pmid:31580259
pmcid:PMC6800002
fatcat:lg3vxbd3bzaqdgg5yrbgmg6kr4