Recognition of shorter and longer trimethyllysine analogues by epigenetic reader proteins

文献情報

出版日 2018-02-09

DOI 10.1039/C8CC01009A

インパクトファクター 6.222

著者

Abbas H. K. Al Temimi, Roman Belle, Kiran Kumar, Peter Betlem, Bas J. G. E. Pieters, Robert S. Paton, Jasmin Mecinović

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要旨

Histone Nε-lysine methylation is a widespread posttranslational modification that is specifically recognised by a diverse class of Nε-methyllysine binding reader proteins. Combined thermodynamic data, molecular dynamics simulations, and quantum chemical studies reveal that reader proteins efficiently bind trimethylornithine and trimethylhomolysine, the simplest Nε-trimethyllysine analogues that differ in the length of the side chain.

掲載誌

Chemical Communications

CiteScore: 8.6

自己引用率: 4.7%

年間論文数: 2458

ChemComm publishes urgent research which is of outstanding significance and interest to experts in the field, while also appealing to the journal’s broad chemistry readership. Our communication format is ideally suited to short, urgent studies that are of such importance that they require accelerated publication. Our scope covers all topics in chemistry, and research at the interface of chemistry and other disciplines (such as materials science, nanoscience, physics, engineering and biology) where there is a significant novelty in the chemistry aspects. Major topic areas covered include: Analytical Chemistry Catalysis Chemical Biology and medicinal chemistry Computational Chemistry and Machine Learning Energy and sustainable chemistry Environmental Chemistry Green Chemistry Inorganic Chemistry Materials Chemistry Nanoscience Organic Chemistry Physical Chemistry Polymer Chemistry Supramolecular Chemistry

Recognition of shorter and longer trimethyllysine analogues by epigenetic reader proteins

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