Movie
Controller
Structure viewers
About Yorodumi Papers
+Search query
-Structure paper
| Title | Structural basis for specific flagellin recognition by the NLR protein NAIP5. |
|---|---|
| Journal, issue, pages | Cell Res, Vol. 28, Issue 1, Page 35-47, Year 2018 |
| Publish date | Nov 28, 2017 |
 Authors | Xinru Yang / Fan Yang / Weiguang Wang / Guangzhong Lin / Zehan Hu / Zhifu Han / Yijun Qi / Liman Zhang / Jiawei Wang / Sen-Fang Sui / Jijie Chai /    |
| PubMed Abstract | The nucleotide-binding domain- and leucine-rich repeat (LRR)-containing proteins (NLRs) function as intracellular immune receptors to detect the presence of pathogen- or host-derived signals. The ...The nucleotide-binding domain- and leucine-rich repeat (LRR)-containing proteins (NLRs) function as intracellular immune receptors to detect the presence of pathogen- or host-derived signals. The mechanisms of how NLRs sense their ligands remain elusive. Here we report the structure of a bacterial flagellin derivative in complex with the NLR proteins NAIP5 and NLRC4 determined by cryo-electron microscopy at 4.28 Å resolution. The structure revealed that the flagellin derivative forms two parallel helices interacting with multiple domains including BIR1 and LRR of NAIP5. Binding to NAIP5 results in a nearly complete burial of the flagellin derivative, thus stabilizing the active conformation of NAIP5. The extreme C-terminal side of the flagellin is anchored to a sterically constrained binding pocket of NAIP5, which likely acts as a structural determinant for discrimination of different bacterial flagellins by NAIP5, a notion further supported by biochemical data. Taken together, our results shed light on the molecular mechanisms underlying NLR ligand perception. |
 External links | Cell Res / PubMed:29182158 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 4.28 Å |
| Structure data | |
| Chemicals |  ChemComp-ATP: |
| Source |
|
 Keywords |  IMMUNE SYSTEM / Flagellin / NAIP5 / NLRC4 / Cryo-EM |
