Crystal structure and mechanism of human lysine-specific demethylase-1

@article{Stavropoulos2006CrystalSA,
  title={Crystal structure and mechanism of human lysine-specific demethylase-1},
  author={Pete Stavropoulos and G{\"u}nter Blobel and Andr{\'e} Hoelz},
  journal={Nature Structural &Molecular Biology},
  year={2006},
  volume={13},
  pages={626-632}
}
The reversible methylation of specific lysine residues in histone tails is crucial in epigenetic gene regulation. LSD1, the first known lysine-specific demethylase, selectively removes monomethyl and dimethyl, but not trimethyl modifications of Lys4 or Lys9 of histone-3. Here, we present the crystal structure of LSD1 at 2.9-Å resolution. LSD1 forms a highly asymmetric, closely packed domain structure from which a long helical 'tower' domain protrudes. The active site cavity is spacious enough… CONTINUE READING
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