Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction.

PLoS One 2018 2;13(1):e0190547. Epub 2018 Jan 2.

Structural Immunobiology Unit, Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, United States of America.

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.

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http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0190547PLOS
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5749810PMC
February 2018
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