Both intra and inter-domain interactions define the intrinsic dynamics and allosteric mechanism in DNMT1s.

ABSTRACT: DNA methyltransferase 1 (DNMT1), a large multidomain enzyme, is believed to be involved in the passive transmission of genomic methylation patterns via methylation maintenance. Yet, the molecular mechanism of interaction networks underlying DNMT1 structures, dynamics, and its biological significance has yet to be fully characterized. In this work, we used an integrated computational strategy that combined coarse-grained and atomistic simulations with coevolution information and network modeling of the residue interactions for the systematic investigation of allosteric dynamics in DNMT1. The elastic network modeling has proposed that the high plasticity of RFTS has strengthened the correlated behaviors of DNMT1 structures through the hinge sites located at the RFTS-CD interface, which media

SUBMITTER: Liang Z 

PROVIDER: S-EPMC7132064 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature