1d01: Difference between revisions
New page: left|200px<br /> <applet load="1d01" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d01, resolution 2.0Å" /> '''STRUCTURE OF TNF REC... |
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[[Image:1d01.gif|left|200px]]<br /> | [[Image:1d01.gif|left|200px]]<br /><applet load="1d01" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1d01, resolution 2.0Å" /> | caption="1d01, resolution 2.0Å" /> | ||
'''STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A HUMAN CD30 PEPTIDE'''<br /> | '''STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A HUMAN CD30 PEPTIDE'''<br /> | ||
==Overview== | ==Overview== | ||
Many members of the tumor necrosis factor receptor (TNFR) superfamily | 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. | ||
==About this Structure== | ==About this Structure== | ||
1D01 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ACE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1D01 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D01 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Kieff, E.]] | [[Category: Kieff, E.]] | ||
[[Category: Kreishman, M.]] | [[Category: Kreishman, M.]] | ||
[[Category: Park, Y | [[Category: Park, Y C.]] | ||
[[Category: Wu, H.]] | [[Category: Wu, H.]] | ||
[[Category: Ye, H.]] | [[Category: Ye, H.]] | ||
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[[Category: protein-peptide complex]] | [[Category: protein-peptide complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:11:28 2008'' |
Revision as of 13:11, 21 February 2008
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STRUCTURE OF TNF RECEPTOR ASSOCIATED FACTOR 2 IN COMPLEX WITH A HUMAN CD30 PEPTIDE
OverviewOverview
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.
About this StructureAbout this Structure
1D01 is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
The structural basis for the recognition of diverse receptor sequences by TRAF2., Ye H, Park YC, Kreishman M, Kieff E, Wu H, Mol Cell. 1999 Sep;4(3):321-30. PMID:10518213
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