Skip to main content
. 2011 Apr 25;108(22):9055–9059. doi: 10.1073/pnas.1019629108

Fig. 1.

Fig. 1.

Multidomain structure of mouse Dnmt1(291–1620). (A) Replication foci targeting sequence (RFTS), zincfinger-like motif (CXXC), bromo-associated homology domain 1 (BAH1) and 2 (BAH2), and catalytic domain are schematically illustrated. The catalytic domain comprising 10 conserved motifs (I ∼ X), and target recognition domain (TRD) between the motifs VIII and IX. The numbers of the amino acid residues are indicated. (B) Ribbon model of mouse Dnmt1(291–1620). Around the C-terminal catalytic domain (blue), the other domains including the RFTS (magenta), CXXC motif (cyan), and two BAH domains BAH1 (green) and BAH2 (orange) are shown. Four zinc ions are shown in red spheres. All of the zinc ions are in a motif similar to Zn-finger motif (Fig. S10). The KG-repeat (1112–1124) linker connecting the N-terminal region and the C-terminal catalytic domain is in a flexible structure as the density map showed disorder.