6GCT
cryo-EM structure of the human neutral amino acid transporter ASCT2
Summary for 6GCT
| Entry DOI | 10.2210/pdb6gct/pdb |
| EMDB information | 4386 |
| Descriptor | Neutral amino acid transporter B(0), GLUTAMINE (2 entities in total) |
| Functional Keywords | neutral amino acid transporter, membrane protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 3 |
| Total formula weight | 170355.14 |
| Authors | Garaeva, A.A.,Oostergetel, G.T.,Gati, C.,Guskov, A.,Paulino, C.,Slotboom, D.J. (deposition date: 2018-04-19, release date: 2018-06-13, Last modification date: 2024-05-15) |
| Primary citation | 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 Cited by 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: 29872227DOI: 10.1038/s41594-018-0076-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.85 Å) |
Structure validation
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