New publication in "Communications Biology"

The human protein lysine methyltransferase NSD2 has very important roles in development and disease but many mechanistic features of this enzyme are unclear. We investigated the substrate sequence specificity of NSD2 and designed an NSD2 super-substrate which is methylated much faster than already known substrates. Molecular dynamics simulations demonstrated that this activity increase is caused by distinct hyperactive conformations of the enzyme-peptide complex. Moreover, we identified ATRX and FANCM as new NSD2 substrates, strengthening the connection of NSD2 with DNA repair.