Dioxygen Binding in the Active Site of Histone Demethylase JMJD2A and the Role of the Protein Environment

Chemistry. 2015 Dec 21;21(52):18869. doi: 10.1002/chem.201504536. Epub 2015 Dec 10.

Abstract

Invited for the cover of this issue is the group of Robert S. Paton at the University of Oxford and his collaborators from Brazil and the Czech Republic. The image depicts histone-enzyme complexation and the chemical interactions inside the active site that define the mode of action. Read the full text of the article at 10.1002/chem.201502983.

MeSH terms

  • Binding Sites
  • Histone Demethylases / chemistry*
  • Histone Demethylases / metabolism
  • Histones / chemistry*
  • Histones / metabolism
  • Jumonji Domain-Containing Histone Demethylases / chemistry*
  • Jumonji Domain-Containing Histone Demethylases / metabolism
  • Protein Binding

Substances

  • Histones
  • Histone Demethylases
  • Jumonji Domain-Containing Histone Demethylases
  • KDM4A protein, human