Crystal structure of TRAIL-DR5 complex identifies a critical role of the unique frame insertion in conferring recognition specificity.

@article{Cha2000CrystalSO,
  title={Crystal structure of TRAIL-DR5 complex identifies a critical role of the unique frame insertion in conferring recognition specificity.},
  author={Sun Shin Cha and B J Sung and Young Ae Kim and Yu Lin Song and Hyun Jin Kim and Seonyoung Kim and Mi Su Lee and Byung Hoon Oh},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 40},
  pages={31171-7}
}
TRAIL is a cytokine that induces apoptosis in a wide variety of tumor cells but rarely in normal cells. It contains an extraordinarily elongated loop because of an unique insertion of 12-16 amino acids compared with the other members of tumor necrosis factor family. Biological implication of the frame insertion has not been clarified. We have determined the crystal structure of TRAIL in a complex with the extracellular domain of death receptor DR5 at 2.2 A resolution. The structure reveals… CONTINUE READING