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

Tengchuan Jin | Zendy; Mo Huang | Zendy; Jiansheng Jiang | Zendy; Patrick Smith | Zendy; Tsan Sam Xiao | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

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

Author(s) -

Tengchuan Jin,

Mo 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 , proinflammatory cytokine , microbiology and biotechnology , receptor , chemistry , maltose binding protein , domain (mathematical analysis) , crystal (programming language) , protein structure , biology , biochemistry , recombinant dna , gene , immunology , paleontology , fusion protein , mathematical analysis , mathematics , computer science , programming language

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research