| Literature DB >> 29457186 |
Abbas H K Al Temimi1, Roman Belle1, Kiran Kumar2, Jordi Poater3, Peter Betlem1, Bas J G E Pieters1, Robert S Paton2, F Matthias Bickelhaupt4, Jasmin Mecinović1.
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.Entities:
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Year: 2018 PMID： 29457186 DOI： 10.1039/c8cc01009a
Source DB: PubMed Journal: Chem Commun (Camb) ISSN： 1359-7345 Impact factor: 6.222