[PDF][PDF] The structural basis for the recognition of diverse receptor sequences by TRAF2

H Ye, YC Park, M Kreishman, E Kieff, H Wu - Molecular cell, 1999 - cell.com
H Ye, YC Park, M Kreishman, E Kieff, H Wu
Molecular cell, 1999cell.com
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 …
Abstract
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.
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