1ca4: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
Line 1: Line 1:
[[Image:1ca4.gif|left|200px]]
[[Image:1ca4.gif|left|200px]]


{{Structure
<!--
|PDB= 1ca4 |SIZE=350|CAPTION= <scene name='initialview01'>1ca4</scene>, resolution 2.2&Aring;
The line below this paragraph, containing "STRUCTURE_1ca4", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND=  
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY=  
or leave the SCENE parameter empty for the default display.
|GENE=
-->
|DOMAIN=
{{STRUCTURE_1ca4| PDB=1ca4  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ca4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ca4 OCA], [http://www.ebi.ac.uk/pdbsum/1ca4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ca4 RCSB]</span>
}}


'''STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 (TRAF2)'''
'''STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 (TRAF2)'''
Line 30: Line 27:
[[Category: Villa, A R.]]
[[Category: Villa, A R.]]
[[Category: Wu, H.]]
[[Category: Wu, H.]]
[[Category: adapter protein]]
[[Category: Adapter protein]]
[[Category: cell survival]]
[[Category: Cell survival]]
[[Category: tnf signaling]]
[[Category: Tnf signaling]]
[[Category: traf]]
[[Category: Traf]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:30:58 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:17:43 2008''

Revision as of 09:31, 2 May 2008

File:1ca4.gif

Template:STRUCTURE 1ca4

STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 (TRAF2)


Overview

Tumour necrosis factor (TNF)-receptor-associated factors (TRAFs) form a family of cytoplasmic adapter proteins that mediate signal transduction from many members of the TNF-receptor superfamily and the interleukin-1 receptor. They are important in the regulation of cell survival and cell death. The carboxy-terminal region of TRAFs (the TRAF domain) is required for self-association and interaction with receptors. The domain contains a predicted coiled-coil region that is followed by a highly conserved TRAF-C domain. Here we report the crystal structure of the TRAF domain of human TRAF2, both alone and in complex with a peptide from TNF receptor-2 (TNF-R2). The structures reveal a trimeric self-association of the TRAF domain, which we confirm by studies in solution. The TRAF-C domain forms a new, eight-stranded antiparallel beta-sandwich structure. The TNF-R2 peptide binds to a conserved shallow surface depression on one TRAF-C domain and does not contact the other protomers of the trimer. The nature of the interaction indicates that an SXXE motif may be a TRAF2-binding consensus sequence. The trimeric structure of the TRAF domain provides an avidity-based explanation for the dependence of TRAF recruitment on the oligomerization of the receptors by their trimeric extracellular ligands.

About this Structure

1CA4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for self-association and receptor recognition of human TRAF2., Park YC, Burkitt V, Villa AR, Tong L, Wu H, Nature. 1999 Apr 8;398(6727):533-8. PMID:10206649 Page seeded by OCA on Fri May 2 12:30:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA