Structural basis for the recognition of Ubc13 by the Shigella flexneri effector OspI.

@article{Nishide2013StructuralBF,
  title={Structural basis for the recognition of Ubc13 by the Shigella flexneri effector OspI.},
  author={Akira Nishide and Minsoo Kim and Kenji Takagi and Ai Himeno and Takahito Sanada and Chihiro Sasakawa and Tsunehiro Mizushima},
  journal={Journal of molecular biology},
  year={2013},
  volume={425 15},
  pages={2623-31}
}
Ubc13 is a ubiquitin-conjugating enzyme that plays a key role in the nuclear factor-κB signal transduction pathway in human diseases. The Shigella flexneri effector OspI affects inflammatory responses by catalyzing the deamidation of a specific glutamine residue at position 100 in Ubc13 during infection. This modification prevents the activation of the TNF (tumor necrosis factor) receptor-associated factor 6, leading to modulation of the diacylglycerol-CBM (CARD-Bcl10-Malt1) complex-TNF… CONTINUE READING

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