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-Structure paper
タイトル | Cryo-EM structure of the human neutral amino acid transporter ASCT2. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 25, Issue 6, Page 515-521, Year 2018 |
掲載日 | 2018年6月5日 |
著者 | Alisa A Garaeva / Gert T Oostergetel / Cornelius Gati / Albert Guskov / Cristina Paulino / Dirk J Slotboom / |
PubMed 要旨 | 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 ...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. Relative to structures of other SLC1 members, ASCT2 is in the most extreme inward-oriented state, with the transport domain largely detached from the central scaffold domain on the cytoplasmic side. This domain detachment may be required for substrate binding and release on the intracellular side of the membrane. |
リンク | Nat Struct Mol Biol / PubMed:29872227 |
手法 | EM (単粒子) |
解像度 | 3.85 Å |
構造データ | |
化合物 | ChemComp-GLN: |
由来 |
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キーワード | MEMBRANE PROTEIN (膜タンパク質) / neutral amino acid transporter |