Recognition of methylated peptides by Drosophila melanogaster polycomb chromodomain.

ABSTRACT: Lysine methylation is one of the important post-translational modifications (PTMs) that regulate protein functions. Up to now, proteomic identification of this PTM remains a challenge due to the lack of effective enrichment methods in mass spectrometry experiments. To address this challenge, we present here a systematic approach to predicting peptides in which lysine residues may be methylated to mediate protein-protein interactions. We used the chromodomain of the polycomb protein in Drosophila melanogaster as a model system to illustrate the success of this approach. We started with molecular dynamics simulations and free energy analyses on the histone peptides complexed with the polycomb chromodomain to understand how the binding specificity is achieved. We next conducted virtual mutage

SUBMITTER: Stein RS 

PROVIDER: S-EPMC4258113 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature