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-Structure paper
| タイトル | Amino acid and viral binding by the high-affinity Cationic Amino acid Transporter 1 (CAT1) from Mus musculus. |
|---|---|
| ジャーナル・号・ページ | Nat Commun, Vol. 17, Issue 1, Year 2026 |
| 掲載日 | 2026年2月16日 |
著者 | Mingda Ye / Zhu Liang / Daming Zhou / Ashley C W Pike / SiYi Wang / Dong Wang / Souvika Bakshi / Laurent Brooke / Eleanor P Williams / Jonathan M Elkins / Benedikt M Kessler / David I Stuart / David B Sauer / ![]() |
| PubMed 要旨 | Arginine, lysine, and ornithine are critical to several fundamental aspects of organismal physiology, including protein structure and function, the urea cycle, and intracellular signaling. These ...Arginine, lysine, and ornithine are critical to several fundamental aspects of organismal physiology, including protein structure and function, the urea cycle, and intracellular signaling. These cationic amino acids are imported by several membrane transporters, most notably the Cationic Amino acid Transporters (CATs) in the SLC7 family. Of these, CAT1 is also the receptor for two orthoretroviruses, and determines the host tropism for these viruses. Here, using a combination of CryoEM and in vitro biochemical techniques, we characterize the substrate recognition and transport of CAT1 from Mus musculus. Further, by determining the structures of MmCAT1 in complex with the receptor binding domain from the Friend Murine Leukemia Virus, we identify the key structural interactions that determine the virus' rodent-specific tropism. |
リンク | Nat Commun / PubMed:41698924 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 2.79 - 3.5 Å |
| 構造データ | EMDB-50668, PDB-9fqt: EMDB-50669, PDB-9fqu: EMDB-50670, PDB-9fqv: EMDB-50671, PDB-9fqw: |
| 化合物 | ![]() ChemComp-NAG: ![]() ChemComp-Y01: ![]() ChemComp-ARG: ![]() ChemComp-HOH: ![]() ChemComp-LYS: ![]() ChemComp-ORN: |
| 由来 |
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キーワード | MEMBRANE PROTEIN / MmCAT1 / FrMLV-RBD / SLC / viral tropism |
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murine leukemia virus (ネズミ白血病ウイルス)
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