6GCT

cryo-EM structure of the human neutral amino acid transporter ASCT2

6GCT の概要

• エントリーDOI: 10.2210/pdb6gct/pdb
• EMDBエントリー: 4386
• 分子名称: Neutral amino acid transporter B(0), GLUTAMINE (2 entities in total)
• 機能のキーワード: neutral amino acid transporter, membrane protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 170355.14

構造登録者

Garaeva, A.A.,Oostergetel, G.T.,Gati, C.,Guskov, A.,Paulino, C.,Slotboom, D.J. (登録日: 2018-04-19, 公開日: 2018-06-13, 最終更新日: 2024-05-15)

主引用文献

Garaeva, A.A.,Oostergetel, G.T.,Gati, C.,Guskov, A.,Paulino, C.,Slotboom, D.J.
Cryo-EM structure of the human neutral amino acid transporter ASCT2.
Nat. Struct. Mol. Biol., 25:515-521, 2018

PubMed Abstract: 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.

PubMed: 29872227
DOI: 10.1038/s41594-018-0076-y

実験手法

ELECTRON MICROSCOPY (3.85 Å)