Structural basis of the recognition of a methylated histone tail by JMJD2A

@article{Chen2007StructuralBO,
  title={Structural basis of the recognition of a methylated histone tail by JMJD2A},
  author={Zhongzhou Chen and J. Zang and J. Kappler and X. Hong and F. Crawford and Qin Wang and F. Lan and Chengyu Jiang and J. Whetstine and S. Dai and K. Hansen and Yang Shi and Gongyi Zhang},
  journal={Proceedings of the National Academy of Sciences},
  year={2007},
  volume={104},
  pages={10818 - 10823}
}
The Jumonji C domain is a catalytic motif that mediates histone lysine demethylation. The Jumonji C-containing oxygenase JMJD2A specifically demethylates tri- and dimethylated lysine-9 and lysine-36 of histone 3 (H3K9/36me3/2). Here we present structures of the JMJD2A catalytic core complexed with methylated H3K36 peptide substrates in the presence of Fe(II) and N-oxalylglycine. We found that the interaction between JMJD2A and peptides largely involves the main chains of the enzyme and the… Expand
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