4IFP

X-ray Crystal Structure of Human NLRP1 CARD Domain

Summary for 4IFP

• Entry DOI: 10.2210/pdb4ifp/pdb
• Related: 3KAT 3VD8
• Related PRD ID: PRD_900001
• Descriptor: Maltose-binding periplasmic protein,NACHT, LRR and PYD domains-containing protein 1, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, MALONATE ION, ... (4 entities in total)
• Functional Keywords: death fold superfamily, inflammasome, signal transduction, innate immune system, immune system
• Biological source: Escherichia coli; More
• Total number of polymer chains: 3
• Total formula weight: 156422.71

Authors

Jin, T.,Curry, J.,Smith, P.,Jiang, J.,Xiao, T. (deposition date: 2012-12-14, release date: 2013-04-03, Last modification date: 2023-09-20)

Primary citation

Jin, T.,Curry, J.,Smith, P.,Jiang, J.,Xiao, T.S.
Structure of the NLRP1 caspase recruitment domain suggests potential mechanisms for its association with procaspase-1.
Proteins, 81:1266-1270, 2013

PubMed Abstract: 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.

PubMed: 23508996
DOI: 10.1002/prot.24287

Experimental method

X-RAY DIFFRACTION (1.9948 Å)