한빛사 논문
Abstract
Chang Min Kim1, Hyunseok Jang1, Hyun Ji Ha, Gi Eob Kim, Hyun Ho Park*
College of Pharmacy, Chung-Ang University, Seoul, 06974, Republic of Korea
1These authors contributed equally to this work.
*Corresponding author
Abstract
Conserved immune cell signaling in fish was recently highlighted by the identification of various immune cell signaling molecules. Tumor necrosis factor (TNF) receptor-associated factor (TRAF) proteins are critical adaptor molecules in immune cell signaling and contain E3 ubiquitin ligase activity. Here, we report the first crystal structure of the TRAF5 TRAF domain from the black rockcod (Notothenia coriiceps; ncTRAF5). Our structure revealed both similarities and differences with mammalian TRAF5. Structural and biochemical analyses indicated that ncTRAF5 forms a functional trimer unit in solution, with a structural flexibility that might be critical for imparting resistance to cold temperature-induced stress. We also found conserved surface residues on ncTRAF5 that might be critical binding hot spots for interaction with various receptors.
Keywords
Innate immunity; TRAF; Cold adaptivity; Protein-protein interaction; Structure
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