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Recognition of shorter and longer trimethyllysine analogues by epigenetic reader proteins

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Abstract

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.

Graphical abstract: Recognition of shorter and longer trimethyllysine analogues by epigenetic reader proteins

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Publication details

The article was received on 05 Feb 2018, accepted on 09 Feb 2018 and first published on 09 Feb 2018


Article type: Communication
DOI: 10.1039/C8CC01009A
Citation: Chem. Commun., 2018, Advance Article
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    Recognition of shorter and longer trimethyllysine analogues by epigenetic reader proteins

    A. H. K. Al Temimi, R. Belle, K. Kumar, J. Poater, P. Betlem, B. J. G. E. Pieters, R. S. Paton, F. M. Bickelhaupt and J. Mecinović, Chem. Commun., 2018, Advance Article , DOI: 10.1039/C8CC01009A

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