Crystal structures of the Tudor domains of human PHF20 reveal novel structural variations on the Royal Family of proteins.

@article{AdamsCioaba2012CrystalSO,
  title={Crystal structures of the Tudor domains of human PHF20 reveal novel structural variations on the Royal Family of proteins.},
  author={Melanie A. Adams-Cioaba and Zhihong Li and Wolfram Tempel and Yahong Guo and Chuanbing Bian and Yanjun Li and Robert E Lam and Jinrong Min},
  journal={FEBS letters},
  year={2012},
  volume={586 6},
  pages={859-65}
}
The human PHD finger protein 20 (PHF20) is a putative transcription factor. While little is known about its cognate cellular role, antibodies against PHF20 are present in sera from patients with hepatocellular carcinoma, glioblastoma and childhood medulloblastula. PHF20 comprises two N-terminal Tudor domains, a central C2H2-link zinc finger domain and a C-terminal zinc-binding PHD domain, and is a component of some MLL methyltransferase complexes. Here, we report the crystal structures of the N… CONTINUE READING

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