Structural basis for the activation of an LRR receptor by a single-disulfide-bridged peptide signal
Yifan Bai, Pei Wei, Lijun Wang, Cheng Chi, Cuicui Du, Zhifu Han, Jinfang Yu, Xiao-Quan Wang, Shuguo Hou, Yu Xiao · 2026
Read Structural basis for the activation of an LRR receptor by a single-disulfide-bridged peptide signal by Yifan Bai, Pei Wei, Lijun Wang, Cheng Chi, Cuicui Du, Zhifu Han, Jinfang Yu, Xiao-Quan Wang, Shuguo Hou, Yu Xiao (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-13261660.txt.
Description
Yifan Bai and co-authors reported in 2026, in letter form, how a tiny plant peptide switches on its receptor to trigger defense. The peptide SCREW2 helps plants fight infection and manage water loss through leaf pores. It carries a single internal sulfur bridge, and whether that bridge matters was unknown.
Binding tests showed the bridged peptide grips the receptor's outer part firmly, while versions without the bridge did not bind at all. A partner protein joined only once the peptide sat in place, completing the active complex. The bridge forms inside one molecule, not between two, even under stress signals. Cell assays echoed the pattern: no bridge, no defense signal. The authors conclude the internal bridge locks the peptide into the one shape the receptor accepts. Their structural account clarifies how this hormone family assembles its switch.
Catalog record
| CREATOR | Yifan Bai, Pei Wei, Lijun Wang, Cheng Chi, Cuicui Du, Zhifu Han, Jinfang Yu, Xiao-Quan Wang, Shuguo Hou, Yu Xiao |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 19 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |