A single BIR domain of XIAP sufficient for inhibiting caspases.

@article{Takahashi1998ASB,
  title={A single BIR domain of XIAP sufficient for inhibiting caspases.},
  author={Ryosuke Takahashi and Quinn L. Deveraux and Ingo Tamm and Kate Welsh and Nuria Assa-Munt and Guy Salvesen and John C. Reed},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 14},
  pages={7787-90}
}
The inhibitor of apoptosis proteins (IAPs) constitute an evolutionarily conserved family of homologous proteins that suppress apoptosis induced by multiple stimuli. Some IAP family proteins, including XIAP, cIAP-1, and cIAP-2, can bind and directly inhibit selected caspases, a group of intracellular cell death proteases. These caspase-inhibiting IAP family proteins all contain three tandem BIR domains followed by a RING zinc finger domain. To determine the structural basis for caspase… CONTINUE READING

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