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

Proteins. 2013 Jul;81(7):1266-70. doi: 10.1002/prot.24287. Epub 2013 Apr 20.


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-helix bundle fold of the NLRP1 CARD, typical of the death domain superfamily. The charge surface of the NLRP1 CARD structure and a procaspase-1 CARD model suggests potential mechanisms for their association through electrostatic attraction.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, N.I.H., Intramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adaptor Proteins, Signal Transducing / chemistry*
  • Apoptosis Regulatory Proteins / chemistry*
  • Caspase 1 / chemistry*
  • Caspases / chemistry
  • Humans
  • Protein Binding*
  • Protein Interaction Maps
  • Protein Structure, Secondary
  • Protein Structure, Tertiary


  • Adaptor Proteins, Signal Transducing
  • Apoptosis Regulatory Proteins
  • NLRP1 protein, human
  • Caspases
  • Caspase 1