Structural basis of BFL-1 for its interaction with BAX and its anti-apoptotic action in mammalian and yeast cells.

@article{Zhang2000StructuralBO,
  title={Structural basis of BFL-1 for its interaction with BAX and its anti-apoptotic action in mammalian and yeast cells.},
  author={Hong Zhang and Sandra W. Cowan-Jacob and Marjo Simonen and William Greenhalf and J. -M. Heim and Bernd Meyhack},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 15},
  pages={11092-9}
}
BFL-1 is the smallest member of the BCL-2 family and has been shown to retard apoptosis in various cell lines. However, the structural basis for its function remains unclear. Molecular modeling showed that BFL-1 could have a similar core structure as BCL-xL, consisting of seven alpha helices, although both proteins share only the conserved BCL-2 homology domains (BH1 and BH2 domains), but otherwise have very limited sequence homology, particularly in the N-terminal region. We demonstrated in… CONTINUE READING

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