Structure of a domain-swapped FOXP3 dimer on DNA and its function in regulatory T cells.

@article{Bandukwala2011StructureOA,
  title={Structure of a domain-swapped FOXP3 dimer on DNA and its function in regulatory T cells.},
  author={Hozefa S. Bandukwala and Yongqing Wu and Markus Feuerer and Yongheng Chen and Bianca A Barboza and Srimoyee Ghosh and James C. Stroud and C. Benoist and Diane Mathis and Anjana Rao and Lin Chen},
  journal={Immunity},
  year={2011},
  volume={34 4},
  pages={479-91}
}
The transcription factor FOXP3 is essential for the suppressive function of regulatory T cells that are required for maintaining self-tolerance. We have solved the crystal structure of the FOXP3 forkhead domain as a ternary complex with the DNA-binding domain of the transcription factor NFAT1 and a DNA oligonucleotide from the interleukin-2 promoter. A striking feature of this structure is that FOXP3 forms a domain-swapped dimer that bridges two molecules of DNA. Structure-guided or autoimmune… CONTINUE READING

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