Structures of the neutral amino acid transporter LAT4 provide insights into antitumor effects of its inhibitor tubeimoside-1
Dian Ding, Yishuo Lu, Jingyi Yang, Hongyi Chen, Peijun Jiang, Yan Jin, Jianyuan Luo, Guangxi Wang, Yuxin Yin · 2026
Read Structures of the neutral amino acid transporter LAT4 provide insights into antitumor effects of its inhibitor tubeimoside-1 by Dian Ding, Yishuo Lu, Jingyi Yang, Hongyi Chen, Peijun Jiang, Yan Jin, Jianyuan Luo, Guangxi Wang, Yuxin Yin (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13269557.txt.
Description
Dian Ding and co-authors picture an amino acid transporter that cancers exploit in this 2026 study. Cutting methionine, a key amino acid, is a rising tactic against cancer and for longer life. The transporter LAT4 pulls that amino acid in and is overactive in many cancers.
No one knew LAT4's shape, and no blocker existed. Using cryo-microscopy, the team solved its structure, plus that of a cousin transporter. A bound phenylalanine revealed the cargo pocket. A plant compound, tubeimoside-1, blocks the transporter, and the structures show how it might work. The maps give drug hunters a foothold against a cancer supply line.
Catalog record
| CREATOR | Dian Ding, Yishuo Lu, Jingyi Yang, Hongyi Chen, Peijun Jiang, Yan Jin, Jianyuan Luo, Guangxi Wang, Yuxin Yin |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 73 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |