Crystal structure of NLRC4 reveals its autoinhibition mechanism.

@article{Hu2013CrystalSO,
  title={Crystal structure of NLRC4 reveals its autoinhibition mechanism.},
  author={Zehan Hu and Chuangye Yan and Peiyuan Liu and Zhiwei Huang and Rui Ma and Chenlu Zhang and Ruiyong Wang and Yueteng Zhang and Fabio Martinon and Di Miao and Haiteng Deng and Jiawei Wang and Junbiao Chang and Jijie Chai},
  journal={Science},
  year={2013},
  volume={341 6142},
  pages={
          172-5
        }
}
Nucleotide-binding and oligomerization domain-like receptor (NLR) proteins oligomerize into multiprotein complexes termed inflammasomes when activated. Their autoinhibition mechanism remains poorly defined. Here, we report the crystal structure of mouse NLRC4 in a closed form. The adenosine diphosphate-mediated interaction between the central nucleotide-binding domain (NBD) and the winged-helix domain (WHD) was critical for stabilizing the closed conformation of NLRC4. The helical domain HD2… CONTINUE READING

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