|
|
| Line 14: |
Line 14: |
| *TRAF1 | | *TRAF1 |
|
| |
|
| **[[3m0d]] – hTRAF1 residues 266-329 + hTRAF2 + cIAP2 - human<br /> | | **[[5e1t]] – hTRAF2 TRAF domain - human<br /> |
| | **[[3m0d]] – hTRAF1 residues 266-329 + hTRAF2 + cIAP2 <br /> |
|
| |
|
| *TRAF2 | | *TRAF2 |
| Line 60: |
Line 61: |
| == References == | | == References == |
| <references/> | | <references/> |
| | [[Category:Topic Page]] |
Revision as of 19:26, 10 October 2017
| Function
TNF receptor-associated factor (TRAF) are signal transducers and are involved in regulation of apoptosis, inflammation and antiviral response. There are 7 known TRAF proteins. All TRAF proteins share a C-terminal homology region named TRAF domain which can bind the cytoplasmic domain of receptors and other TRAF proteins[1]. TRAF1 is the only TRAF which does not have N-terminal RING and zinc finger motifs. TRAF2, TRAF5 and TRAF6 mediate activation of NF-κB and JNK. TRAF3 mediates some innate immune receptor signals and regulates some post-translational modifications[2]. TRAF4 is a binding partner of glycoproteins in platelets[3].
Structural highlights
The interaction of TRAF2 with the adaptor protein TRADD is bipartite with one part containing mainly hydrophobic interactions while the second part contains mainly polar interactions[4]. Hydrophobic, Polar
- ↑ Bradley JR, Pober JS. Tumor necrosis factor receptor-associated factors (TRAFs). Oncogene. 2001 Oct 1;20(44):6482-91. PMID:11607847 doi:https://dx.doi.org/10.1038/sj.onc.1204788
- ↑ Hildebrand JM, Yi Z, Buchta CM, Poovassery J, Stunz LL, Bishop GA. Roles of tumor necrosis factor receptor associated factor 3 (TRAF3) and TRAF5 in immune cell functions. Immunol Rev. 2011 Nov;244(1):55-74. doi: 10.1111/j.1600-065X.2011.01055.x. PMID:22017431 doi:https://dx.doi.org/10.1111/j.1600-065X.2011.01055.x
- ↑ Arthur JF, Shen Y, Gardiner EE, Coleman L, Murphy D, Kenny D, Andrews RK, Berndt MC. TNF receptor-associated factor 4 (TRAF4) is a novel binding partner of glycoprotein Ib and glycoprotein VI in human platelets. J Thromb Haemost. 2011 Jan;9(1):163-72. doi: 10.1111/j.1538-7836.2010.04091.x. PMID:20946164 doi:https://dx.doi.org/10.1111/j.1538-7836.2010.04091.x
- ↑ Park YC, Ye H, Hsia C, Segal D, Rich RL, Liou HC, Myszka DG, Wu H. A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction. Cell. 2000 Jun 23;101(7):777-87. PMID:10892748
|
3D Structures of TNF receptor-associated factor
Updated on 10-October-2017
{"openlevels":0}
- TRAF1
- 5e1t – hTRAF2 TRAF domain - human
- 3m0d – hTRAF1 residues 266-329 + hTRAF2 + cIAP2
- TRAF2
- 1ca4 – hTRAF2 TRAF domain residues 334-501
- 3knv – hTRAF2 RING+zinc finger 1 domains residues 1-133
- 3m06 – hTRAF2 residues 266-329
- TRAF2 complex with peptide
- 1ca9 – hTRAF2 TRAF domain + TNF-R2 peptide
- 1qsc, 1d00, 1czz – hTRAF2 TRAF domain + CD40 receptor peptide
- 1d01 – hTRAF2 TRAF domain + CD30 peptide
- 1czy – hTRAF2 TRAF domain + latent membrane protein peptide
- 1d0a – hTRAF2 TRAF domain + OX40L receptor peptide
- 1d0j – hTRAF2 TRAF domain + 4-1BB ligand receptor peptide
- 1f3v – hTRAF2 TRAF domain + TRADD N terminal
- 3m0a – hTRAF2 residues 266-329 + cIAP2
- TRAF3
- 4ghu – TRAF3 TRAF domain residues 376-567 + antiviral-signaling protein peptide - mouse
- TRAF4
- TRAF5
- 4gjh – hTRAF5 TRAF domain residues 381-558
- TRAF6
- 1lb4 – hTRAF6 TRAF domain
- 2jmd, 2eci – hTRAF6 RING domain - NMR
- 3hcs – hTRAF6 RING+zinc finger 1-3 domains
- TRAF6 complex with peptide
- 1lb5 – hTRAF6 TRAF domain + RANK peptide
- 1lb6 – hTRAF6 TRAF domain + CD40 antigen peptide
- 3hct, 3hcu – hTRAF6 RING+zinc finger 1 domains + ubiquitin-conjugating enzyme E2
- 4z8m – hTRAF6 TRAF domain + antiviral-signaling protein peptide
References
