Figure 1.

Solution structure of MBD4_MBD bound to methylated DNA. (a) A best-fit superimposition stereo cartoon diagram depicts the twenty calculated structures of the MBD4_MBD (yellow) and DNA (green) with key interacting protein residues shown as stick diagrams. (b) A cartoon diagram depicts the lowest energy structure of MBD4_MBD (yellow) and DNA (green) with key interacting protein residues shown as stick diagrams. (c) A best-fit superimposition cartoon diagram of the MBD4_MBD (yellow), MeCP2_MBD (blue) and cMBD2_MBD (green) shows that the C-terminal α-helix is longer in MeCP2 and MBD4 as compared to cMBD2. Horizontal bars below the diagram highlight the relative lengths of this α-helix in each. (d) An expanded mixed rendering diagram shows critical interactions involved in DNA binding with key residues shown as sticks and potential hydrogen bonds highlighted with yellow dashed lines. Note that Tyr¹⁰⁹ points away from DNA, which differs from other MBD proteins.