Recognition of shorter and longer trimethyllysine analogues by epigenetic reader proteins.

Abbas H K Al TemimiRoman BelleKiran Kumar Jordi PoaterPeter BetlemBas J G E PietersRobert S Paton Friedrich Matthias Bickelhaupt Jasmin Mecinovic

Published in: Chemical communications (Cambridge, England) (2018)

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.

Keyphrases

molecular dynamics simulations
molecular docking
dna methylation
genome wide
gene expression
molecular dynamics
big data
transcription factor
aqueous solution