Structural mechanisms of DIAP1 auto-inhibition and DIAP1-mediated inhibition of drICE.

@article{Li2011StructuralMO,
  title={Structural mechanisms of DIAP1 auto-inhibition and DIAP1-mediated inhibition of drICE.},
  author={Xiaochun Li and Jiawei Wang and Yigong Shi},
  journal={Nature communications},
  year={2011},
  volume={2},
  pages={408}
}
The Drosophila inhibitor of apoptosis protein DIAP1 exists in an auto-inhibited conformation, unable to suppress the effector caspase drICE. Auto-inhibition is disabled by caspase-mediated cleavage of DIAP1 after Asp20. The cleaved DIAP1 binds to mature drICE, inhibits its protease activity, and, presumably, also targets drICE for ubiquitylation. DIAP1-mediated suppression of drICE is effectively antagonized by the pro-apoptotic proteins Reaper, Hid, and Grim (RHG). Despite rigorous effort, the… CONTINUE READING
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