6KU5
Notothenia coriiceps TRAF5
Summary for 6KU5
| Entry DOI | 10.2210/pdb6ku5/pdb |
| Descriptor | TRAF5 (1 entity in total) |
| Functional Keywords | traf, tumor necrosis factor receptor association factor, notothenia coriiceps traf5, protein binding |
| Biological source | Notothenia coriiceps |
| Total number of polymer chains | 2 |
| Total formula weight | 46132.49 |
| Authors | Park, H.H.,Kim, C.M. (deposition date: 2019-08-30, release date: 2020-07-08, Last modification date: 2024-03-27) |
| Primary citation | Kim, 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: 32283248DOI: 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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