The structural basis for the recognition of diverse receptor sequences by TRAF2.

@article{Ye1999TheSB,
  title={The structural basis for the recognition of diverse receptor sequences by TRAF2.},
  author={Hong Ye and Young Chul Park and Mara Kreishman and Elliott Kieff and Hao Wu},
  journal={Molecular cell},
  year={1999},
  volume={4 3},
  pages={321-30}
}
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… CONTINUE READING

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