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

• Published in: Chemistry : a European journal Vol. 21; no. 52; p. 18869
• Main Authors: Cortopassi, Wilian A., Simion, Robert, Honsby, Charles E., França, Tanos C. C., Paton, Robert S.
• Format: Journal Article
• Language: English
• Published: Weinheim WILEY-VCH Verlag 21.12.2015; WILEY‐VCH Verlag; Wiley Subscription Services, Inc
• Subjects: Binding; Binding Sites; Brazil; Chemical interactions; Chemistry; Complexation; Computation; Histone Demethylases - chemistry; Histone Demethylases - metabolism; Histones; Histones - chemistry; Histones - metabolism; Jumonji Domain-Containing Histone Demethylases - chemistry; Jumonji Domain-Containing Histone Demethylases - metabolism; Mode of action; Protein Binding; Proteins; State of the art; Texts
• ISSN: 0947-6539; 1521-3765
• DOI: 10.1002/chem.201504536

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. “Our work focuses on using state of the art computational techniques to understand the role of the protein environment of an epigenetic “eraser” process.” Read more about the story behind the cover in the Cover Profile and about the research itself on page 18983 ff. (DOI: 10.1002/chem.201502983).