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6KU5

Notothenia coriiceps TRAF5

Summary for 6KU5
Entry DOI10.2210/pdb6ku5/pdb
DescriptorTRAF5 (1 entity in total)
Functional Keywordstraf, tumor necrosis factor receptor association factor, notothenia coriiceps traf5, protein binding
Biological sourceNotothenia coriiceps
Total number of polymer chains2
Total formula weight46132.49
Authors
Park, H.H.,Kim, C.M. (deposition date: 2019-08-30, release date: 2020-07-08, Last modification date: 2024-03-27)
Primary citationKim, C.M.,Jang, H.,Ha, H.J.,Kim, G.E.,Park, H.H.
Structural and biochemical characterization of TRAF5 from Notothenia coriiceps and its implications in fish immune cell signaling.
Fish Shellfish Immunol., 102:56-63, 2020
Cited by
PubMed 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.
PubMed: 32283248
DOI: 10.1016/j.fsi.2020.04.016
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.299 Å)
Structure validation

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