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. 2018 Dec 11;9(12):620. doi: 10.3390/genes9120620

Figure 7.

Figure 7

Structural analysis of the Atrx-Dnmt3-Dnmt3l (ADD) domain-mediated DNMT3A autoinhibition. (A) Structural overview of the DNMT3A-DNMT3L tetramer, with the DNMT3A fragment comprised of both the ADD and MTase domains (PDB 4U7P). (B) Intramolecular interactions between the ADD loop (blue) and the MTase domain (aquamarine) of DNMT3A. The hydrogen bonding interactions are depicted as dashed lines. (C) The ADD-binding site of the DNMT3A MTase overlaps with its DNA binding site. (D) Structure of the DNMT3A-DNMT3L tetramer bound to the histone H3K4me0 peptide (PDB 4U7T), with the interaction between H3K4me0 and the ADD domain shown in an expanded view (PDB 3A1B).