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Structural basis for specific flagellin recognition by the NLR protein NAIP5.


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 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.

SUBMITTER: Yang X 

PROVIDER: S-EPMC5752844 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature

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Structural basis for specific flagellin recognition by the NLR protein NAIP5.

Yang Xinru X   Yang Fan F   Wang Weiguang W   Lin Guangzhong G   Hu Zehan Z   Han Zhifu Z   Qi Yijun Y   Zhang Liman L   Wang Jiawei J   Sui Sen-Fang SF   Chai Jijie J  

Cell research 20171128 1


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 paralle  ...[more]

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