1czy
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(New page: 200px<br /> <applet load="1czy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1czy, resolution 2.00Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 14:20, 12 November 2007
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CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE TRAF DOMAIN OF HUMAN TRAF2 AND AN LMP1 BINDING 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.
About this Structure
1CZY is a Protein complex structure of sequences from Homo sapiens with ACE as ligand. Full crystallographic information is available from OCA.
Reference
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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