Insights into interferon regulatory factor activation from the crystal structure of dimeric IRF5

@article{Chen2008InsightsII,
  title={Insights into interferon regulatory factor activation from the crystal structure of dimeric IRF5},
  author={Weijun Chen and Suvana S. Lam and Hema Srinath and Zhaozhao Jiang and John J. Correia and Celia A Schiffer and Katherine A. Fitzgerald and Kai Lin and William E. Royer},
  journal={Nature Structural &Molecular Biology},
  year={2008},
  volume={15},
  pages={1213-1220}
}
Interferon regulatory factors (IRFs) are essential in the innate immune response and other physiological processes. Activation of these proteins in the cytoplasm is triggered by phosphorylation of serine and threonine residues in a C-terminal autoinhibitory region, which stimulates dimerization, transport into the nucleus, assembly with the coactivator CBP/p300 and initiation of transcription. The crystal structure of the transactivation domain of pseudophosphorylated human IRF5 strikingly… CONTINUE READING
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