Open AccessCrystal structure of human NLRP12 PYD domain and implication in homotypic interaction
Author(s) -
Tengchuan Jin,
M. Huang,
Jiansheng Jiang,
Patrick Smith,
Tsan Sam Xiao
Publication year - 2018
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0190547
Subject(s) - context (archaeology) , inflammation , chemistry , microbiology and biotechnology , maltose binding protein , proinflammatory cytokine , receptor , protein structure , crystal structure , biology , biochemistry , biophysics , crystallography , recombinant dna , gene , immunology , paleontology , fusion protein
NLRP12 is a NOD-like receptor that plays multiple roles in both inflammation and tumorigenesis. Despite the importance, little is known about its mechanism of action at the molecular level. Here, we report the crystal structure of NLRP12 PYD domain at 1.70 Å fused with an maltose-binding protein (MBP) tag. Interestingly, the PYD domain forms a dimeric configuration through a disulfide bond in the crystal. The possible biological significance is discussed in the context of ROS induced NF-κB activation.