Exploring the bistable equilibrium of methylated CpG DNA recognition by the MBD2 protein.

ABSTRACT: Methyl-CpG binding domain 2 (MBD2) is a critical epigenetic regulator that recognizes and binds with high selectivity to methylated CpG dinucleotides, a fundamental epigenetic mark involved in gene regulation and chromatin organization. Therefore, understanding the interactions and conformational dynamics that drive MBD2's high selectivity and strong binding affinity to methylated CpG is crucial to unraveling its regulatory mechanisms. In this study, through extensive classical MD simulations, we investigated the formation of the methylated CpG-MBD2 recognition complex. By positioning MBD2 one base pair downstream of its target mCpG site, we observed its transition to a stable complex at the target site within the microsecond timescale. Significantly, we observe that upon binding to methyl

SUBMITTER: Volkenandt S 

PROVIDER: S-EPMC12236691 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature