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CryoEM study of NLR proteins in the immune regulation


EMSL Project ID
51819

Abstract

Nucleotide-binding domain and leucine rich repeat containing (NLR) proteins comprise a fascinating family that plays key roles in regulating immune signal transduction: they initiate inflammation in response to pathogens and danger signals by forming the NLR inflammasomes, and control MHC gene transcription. The human NLRs share a three-domain organization, including the N-terminal domain (NTD), the middle nucleotide-binding domain (NBD), and the C-terminal leucine-rich repeat (LRR) domain. These three domains mediate NLRs functions through ligand binding, protein-protein interaction and protein oligomerization. In this study, we propose to systematically study the molecular mechanism underlying NLRs in immune signal transduction. Having resolved the cryo-EM structure of the NAIP/NLRC4 inflammasome, we will apply our expertise to the future investigation of NLR proteins. The proposed research will yield fundamental insights into NLR signaling and create translational value for therapeutic development against immune diseases.

Project Details

Start Date
2021-02-15
End Date
2021-03-17
Status
Closed

Team

Principal Investigator

Liman Zhang
Institution
Oregon Health & Science University

Team Members

Bhaskar Paidimuddala
Institution
Oregon Health & Science University

Jianhao Cao
Institution
Oregon Health & Science University