Inter-domain distance analysis reveals conformational changes in the Keap1-Nrf2 stress sensor system
Ritsumi Saito, Takeshi Kawabata, Seisuke Yamashita, Keisuke Oki, Takashi Fujii, Hiroki Kawauchi, Yoshiaki Doi, Machiko Irie, Takuya Torizawa, Kengo Kinoshita, Masayuki Yamamoto, Seizo Koshiba · 2026
Read Inter-domain distance analysis reveals conformational changes in the Keap1-Nrf2 stress sensor system by Ritsumi Saito, Takeshi Kawabata, Seisuke Yamashita, Keisuke Oki, Takashi Fujii, Hiroki Kawauchi, Yoshiaki Doi, Machiko Irie, Takuya Torizawa, Kengo Kinoshita, Masayuki Yamamoto, Seizo Koshiba (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-13571941.txt.
Description
Ritsumi Saito and eleven co-authors map the moving shape of a cell defense switch. Their 2026 study examines the Keap1-Nrf2 system, which guards cells against oxidative stress. Keap1 is a flexible protein built from two matching halves. Its bendiness has blocked a full picture of its structure for years.
Using cryo-electron microscopy, the team found Keap1 in many poses, though the particles lined up awkwardly in the ice. They built a method that measures the gap between the two tail domains of the paired protein. That gap shifted when Nrf2 bound, or when binding was blocked. Cutting out three flexible stretches showed each one feeds the protein's bendiness. The findings guide drugs aimed at this stress switch.
Catalog record
| CREATOR | Ritsumi Saito, Takeshi Kawabata, Seisuke Yamashita, Keisuke Oki, Takashi Fujii, Hiroki Kawauchi, Yoshiaki Doi, Machiko Irie, Takuya Torizawa, Kengo Kinoshita, Masayuki Yamamoto, Seizo Koshiba |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 73 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |