Histone-binding of DPF2 mediates its repressive role in myeloid differentiation.

@article{Huber2017HistonebindingOD,
  title={Histone-binding of DPF2 mediates its repressive role in myeloid differentiation.},
  author={Ferdinand M. Huber and Sarah M. Greenblatt and Andrew Mitsunori Davenport and Concepci{\'o}n S{\'a}nchez Mart{\'i}nez and Ye Xu and Ly P. Vu and Stephen D. Nimer and Andr{\'e} Hoelz},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2017},
  volume={114 23},
  pages={
          6016-6021
        }
}
Double plant homeodomain finger 2 (DPF2) is a highly evolutionarily conserved member of the d4 protein family that is ubiquitously expressed in human tissues and was recently shown to inhibit the myeloid differentiation of hematopoietic stem/progenitor and acute myelogenous leukemia cells. Here, we present the crystal structure of the tandem plant homeodomain finger domain of human DPF2 at 1.6-Å resolution. We show that DPF2 interacts with the acetylated tails of both histones 3 and 4 via… CONTINUE READING
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