4ifp | pdb_00004ifp

X-ray Crystal Structure of Human NLRP1 CARD Domain

spinqualitylabelsall models 4ifp, resolution 1.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4ifp is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MAL, MLI Related: 3kat, 3vd8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. Publication Abstract from PubMed 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 A 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. Proteins 2013. (c) 2013 Wiley Periodicals, Inc. Structure of the NLRP1 caspase recruitment domain suggests potential mechanisms for its association with procaspase-1.,Jin T, Curry J, Smith P, Jiang J, Xiao TS Proteins. 2013 Mar 18. doi: 10.1002/prot.24287. PMID:23508996 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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