Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet.

@article{Kwon2003MechanismOH,
  title={Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet.},
  author={Taewoo Kwon and Jeong Ho Chang and Eunyee Kwak and Chang Wook Lee and Andrzej Joachimiak and Young Chang Kim and Jaewoon Lee and Yunje Cho},
  journal={The EMBO journal},
  year={2003},
  volume={22 2},
  pages={292-303}
}
The methylation of lysine residues of histones plays a pivotal role in the regulation of chromatin structure and gene expression. Here, we report two crystal structures of SET7/9, a histone methyltransferase (HMTase) that transfers methyl groups to Lys4 of histone H3, in complex with S-adenosyl-L-methionine (AdoMet) determined at 1.7 and 2.3 A resolution. The structures reveal an active site consisting of: (i) a binding pocket between the SET domain and a c-SET helix where an AdoMet molecule in… CONTINUE READING

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