Structure of the NLRP1 caspase recruitment domain suggests potential mechanisms for its association with procaspase-1.

@article{Jin2013StructureOT,
  title={Structure of the NLRP1 caspase recruitment domain suggests potential mechanisms for its association with procaspase-1.},
  author={Tengchuan Jin and James Curry and Patrick H. Smith and Jiansheng Jiang and Tsan Sam Xiao},
  journal={Proteins},
  year={2013},
  volume={81 7},
  pages={1266-70}
}
The NLRP1 inflammasome responds to microbial challenges such as Bacillus anthracis infection and is implicated in autoimmune disease such as vitiligo. Human NLRP1 contains both an N-terminal pyrin domain (PYD) and a C-terminal caspase recruitment domain (CARD), with the latter being essential for its association with the downstream effector procaspase-1. Here we report a 2.0 Å crystal structure of the human NLRP1 CARD as a fusion with the maltose-binding protein. The structure reveals the six… CONTINUE READING
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