Investigating D-lysine stereochemistry for epigenetic methylation, demethylation and recognition

Autor:	Akane Kawamura, Roman Belle, James E. Dunford, Christopher J. Schofield, Udo Oppermann, Tom Brown, Jasmin Mecinović, Catrine Johansson, Kiran Kumar, Al Temimi Ahk., Richard J. Hopkinson, Pieters Bjge., Robert S. Paton, Anthony Tumber
Rok vydání:	2017
Předmět:	Models Molecular 0301 basic medicine Histone lysine methylation Molecular Conformation Synthetic Organic Chemistry Methylation complex mixtures Article Catalysis Epigenesis Genetic 03 medical and health sciences Materials Chemistry Histone code Epigenomics Histone Demethylases biology Chemistry Lysine EZH2 Metals and Alloys Stereoisomerism Methyltransferases General Chemistry Surfaces Coatings and Films Electronic Optical and Magnetic Materials 030104 developmental biology Histone Biochemistry Histone methyltransferase Biocatalysis Ceramics and Composites biology.protein ComputingMethodologies_DOCUMENTANDTEXTPROCESSING Thermodynamics bacteria Physical Organic Chemistry
Zdroj:	Chemical Communications, 53, 99, pp. 13264-13267 Chemical Communications, 53, 13264-13267 Chemical Communications
ISSN:	1359-7345
Popis:	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 and identify key electrostatic interactions involved.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32311f0ea9a4d4b9ed175b875f43e7c9 https://hdl.handle.net/2066/181125 Zobrazit plný text záznamu