1d0j: Difference between revisions

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[[Image:1d0j.~~gif~~|left|200px]]

[[Image:1d0j.png|left|200px]]

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~~'''~~STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A M4-1BB PEPTIDE~~'''~~

===STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A M4-1BB PEPTIDE===

~~==Overview==~~

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Many members of the tumor necrosis factor receptor (TNFR) superfamily initiate intracellular signaling by recruiting TNFR-associated factors (TRAFs) through their cytoplasmic tails. TRAFs apparently recognize highly diverse receptor sequences. Crystal structures of the TRAF domain of human TRAF2 in complex with peptides from the TNFR family members CD40, ~~CD30~~, ~~Ox40, 4-1BB, and~~ the ~~EBV oncoprotein LMP1 revealed a conserved binding mode. A major TRAF2-binding consensus sequence,~~ (P/S/~~A/T)x(Q/E~~)E, ~~and a minor consensus motif, PxQxxD, can be defined from~~ the ~~structural analysis, which encompass all known TRAF2~~-~~binding sequences. The structural information provides a template for the further dissection of receptor binding specificity of TRAF2 and for the understanding of the complexity of TRAF~~-~~mediated signal transduction.~~

The line below this paragraph, {{ABSTRACT_PUBMED_10518213}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10518213 is the PubMed ID number.

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==About this Structure==

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[[Category: B-sandwich]]

[[Category: Protein-peptide complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 13~~:18:44 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:56:59 2008''

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-[[Image:1d0j.gif|left|200px]]
+{{Seed}}
+[[Image:1d0j.png|left|200px]]
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 {{STRUCTURE_1d0j|  PDB=1d0j  |  SCENE=  }}
-'''STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A M4-1BB PEPTIDE'''
+===STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A M4-1BB PEPTIDE===
-==Overview==
+<!--
-Many members of the tumor necrosis factor receptor (TNFR) superfamily initiate intracellular signaling by recruiting TNFR-associated factors (TRAFs) through their cytoplasmic tails. TRAFs apparently recognize highly diverse receptor sequences. Crystal structures of the TRAF domain of human TRAF2 in complex with peptides from the TNFR family members CD40, CD30, Ox40, 4-1BB, and the EBV oncoprotein LMP1 revealed a conserved binding mode. A major TRAF2-binding consensus sequence, (P/S/A/T)x(Q/E)E, and a minor consensus motif, PxQxxD, can be defined from the structural analysis, which encompass all known TRAF2-binding sequences. The structural information provides a template for the further dissection of receptor binding specificity of TRAF2 and for the understanding of the complexity of TRAF-mediated signal transduction.
+The line below this paragraph, {{ABSTRACT_PUBMED_10518213}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10518213 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10518213}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: B-sandwich]]
 [[Category: Protein-peptide complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:18:44 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:56:59 2008''