TNF receptor-associated factor: Difference between revisions

From Proteopedia
Jump to navigationJump to search
Michal Harel (talk | contribs)
No edit summary
Michal Harel (talk | contribs)
No edit summary
 
(12 intermediate revisions by 3 users not shown)
Line 1: Line 1:
<StructureSection load='1f3v' size='340' side='right' caption='Human TRAF2 TRAF domain (green) complex with TNFR type 1 associated death domain protein TRADD (grey) (PDB code [[1d01]])' scene=''>
<StructureSection load='' size='350' side='right' caption='Human TRAF2 TRAF domain (green) complex with TNFR type 1 associated death domain protein TRADD (deepskyblue) (PDB code [[1f3v]])' scene='70/708054/Cv/1'>
__TOC__
== Function ==
== 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<ref>PMID:11607847</ref>.  '''TRAF2-6''' have N-terminal RING and zinc finger motifs.  '''TRAF2, TRAF5 and TRAF6''' mediate activation of NF-κB and JNK.
'''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<ref>PMID:11607847</ref>.   
*'''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<ref>PMID:22017431</ref>. 
*'''TRAF4''' is a binding partner of glycoproteins in platelets<ref>PMID:20946164</ref>.


== Structural highlights ==
== 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<ref>PMID:10892748</ref>.
The interaction of TRAF2 with the adaptor protein TRADD is <scene name='70/708054/Cv/4'>bipartite with one part containing mainly hydrophobic interactions while the second part contains mainly polar interactions</scene><ref>PMID:10892748</ref>. {{Template:ColorKey_Hydrophobic}},  {{Template:ColorKey_Polar}}
</StructureSection>
 
== 3D Structures of TNF receptor-associated factor ==
== 3D Structures of TNF receptor-associated factor ==
[[TNF receptor-associated factor 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*TRAF1
 
**[[3m0d]] – hTRAF1 residues 266-329 + hTRAF2 + cIAP2 - human<br />
 
*TRAF2
 
**[[1ca4]] – hTRAF2 TRAF domain residues 334-501<br />
**[[3knv]] – hTRAF2 RING+zinc finger 1 domains residues 1-133 <br />
**[[3m06]] – hTRAF2 residues 266-329 <br />
 
*TRAF2 complex with peptide
 
**[[1ca9]] – hTRAF2 TRAF domain + TNF-R2 peptide<br />
**[[1qsc]], [[1d00]], [[1czz]] – hTRAF2 TRAF domain + CD40 receptor peptide<br />
**[[1d01]] – hTRAF2 TRAF domain + CD30 peptide<br />
**[[1czy]] – hTRAF2 TRAF domain + latent membrane protein peptide<br />
**[[1d0a]] – hTRAF2 TRAF domain + OX40L receptor peptide<br />
**[[1d0j]] – hTRAF2 TRAF domain + 4-1BB ligand receptor peptide<br />
**[[1f3v]] – hTRAF2 TRAF domain + TRADD N terminal<br />
**[[3m0a]] – hTRAF2 residues 266-329 + cIAP2<br />
 
*TRAF6
 
**[[1lb4]] – hTRAF6 TRAF domain <br />
**[[2jmd]], [[2eci]] – hTRAF6 RING domain - NMR<br />
**[[3hcs]] – hTRAF6 RING+zinc finger 1-3 domains <br />
 
*TRAF6 complex with peptide


**[[1lb5]] – hTRAF6 TRAF domain + RANK peptide<br />
**[[1lb6]] – hTRAF6 TRAF domain + CD40 antigen peptide<br />
**[[3hct]], [[3hcu]] – hTRAF6 RING+zinc finger 1 domains + ubiquitin-conjugating enzyme E2<br />
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]