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-Structure paper
タイトル | Structural basis for specific flagellin recognition by the NLR protein NAIP5. |
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ジャーナル・号・ページ | Cell Res, Vol. 28, Issue 1, Page 35-47, Year 2018 |
掲載日 | 2017年11月28日 |
著者 | Xinru Yang / Fan Yang / Weiguang Wang / Guangzhong Lin / Zehan Hu / Zhifu Han / Yijun Qi / Liman Zhang / Jiawei Wang / Sen-Fang Sui / Jijie Chai / |
PubMed 要旨 | 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. |
リンク | Cell Res / PubMed:29182158 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 4.28 Å |
構造データ | |
化合物 | ChemComp-ATP: |
由来 |
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キーワード | IMMUNE SYSTEM / Flagellin / NAIP5 / NLRC4 / Cryo-EM |