Recognition of shorter and longer trimethyllysine analogues by epigenetic reader proteins.
نویسندگان
چکیده
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.
منابع مشابه
Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins
A large number of structurally diverse epigenetic reader proteins specifically recognize methylated lysine residues on histone proteins. Here we describe comparative thermodynamic, structural and computational studies on recognition of the positively charged natural trimethyllysine and its neutral analogues by reader proteins. This work provides experimental and theoretical evidence that reader...
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ورودعنوان ژورنال:
- Chemical communications
دوره 54 19 شماره
صفحات -
تاریخ انتشار 2018