| Literature DB >> 29186216 |
Roman Belle1, Abbas H K Al Temimi, Kiran Kumar, Bas J G E Pieters, Anthony Tumber, James E Dunford, Catrine Johansson, Udo Oppermann, Tom Brown, Christopher J Schofield, Richard J Hopkinson, Robert S Paton, Akane Kawamura, Jasmin Mecinović.
Abstract
Histone lysine methylation is regulated by Nε-methyltransferases, demethylases, and Nε-methyl lysine binding proteins. Thermodynamic, catalytic and computational studies were carried out to investigate the interaction of three epigenetic protein classes with synthetic histone substrates containing l- and d-lysine residues. The results reveal that out of the three classes, Nε-methyl lysine binding proteins are superior in accepting lysines with the d-configuration.Entities:
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Year: 2017 PMID: 29186216 PMCID: PMC6345366 DOI: 10.1039/c7cc08028j
Source DB: PubMed Journal: Chem Commun (Camb) ISSN: 1359-7345 Impact factor: 6.222