Fig. 3: MD reveals altered structural flexibility of Dnmt3L variants. | Experimental & Molecular Medicine

Fig. 3: MD reveals altered structural flexibility of Dnmt3L variants.

From: Uncovering the acetylation sites of Dnmt3L that regulate protein stability and differentiation potency in embryonic stem cells

Fig. 3: MD reveals altered structural flexibility of Dnmt3L variants.

a Structure of the Dnmt3A–Dnmt3L complex highlighting the Dnmt3L mutation sites K238 and K412. b RMSD profiles over 500-ns simulations, illustrating structural fluctuations of WT Ac Dnmt3L and the other mutants. c Bar plot showing the standard deviation values of RMSD (after 100 ns), indicating that overall flexibility was higher in both mutants than in WT Ac Dnmt3L. d RMSF per residue, indicating local flexibility differences across the protein sequence. e, f SMD pulling simulations. Pulling force profiles comparing WT Ac Dnmt3L with each mutant, showing the time-dependent force experienced during pulling simulations (e) and peak pulling forces extracted from SMD simulations, indicating that mechanical resistance was comparable among WT Ac Dnmt3L and mutant complexes (f). See also Supplementary Fig. 4.

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