Structural analysis of a functional DIAP1 fragment bound to grim and hid peptides.

@article{Wu2001StructuralAO,
  title={Structural analysis of a functional DIAP1 fragment bound to grim and hid peptides.},
  author={Jian-Zhong Wu and Amy E. Cocina and Jijie Chai and Bruce A Hay and Yigong Shi},
  journal={Molecular cell},
  year={2001},
  volume={8 1},
  pages={95-104}
}
The inhibitor of apoptosis protein DIAP1 suppresses apoptosis in Drosophila, with the second BIR domain (BIR2) playing an important role. Three proteins, Hid, Grim, and Reaper, promote apoptosis, in part by binding to DIAP1 through their conserved N-terminal sequences. The crystal structures of DIAP1-BIR2 by itself and in complex with the N-terminal peptides from Hid and Grim reveal that these peptides bind a surface groove on DIAP1, with the first four amino acids mimicking the binding of the… CONTINUE READING

From This Paper

Topics from this paper.
48 Citations
52 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 48 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 52 references

A conserved XIAP-interaction motif in caspase-9 and Smac/ DIABLO mediates opposing effects on caspase activity and apoptosis

  • S. M. Srinivasula, A. Saleh, +7 authors E. S. Alnemri
  • Nature 409, 112–116.
  • 2001
Highly Influential
4 Excerpts

Similar Papers

Loading similar papers…