Sandbox Reserved 1759: Difference between revisions

The MBD protein is composed of alpha helix, parallel and anti-parrallel beta sheet, and random coils. The protein consists of two major subunits with a 60% alpha helixes and 40% beta sheets when viewing the tertiary <scene name='93/934003/60_alpha_and_40_beta/1'>structure</scene>. The alpha helixes and beta sheets within each individual subunit loop and fold to form a <scene name='93/934003/Space_filling/1'>3D globular protein</scene>. The two subunits of the protein are homodimers, containing essentially identical alpha helixes and beta sheets between the two subunits, with intermolecular forces such as hydrogen bonds connecting them. The proteins contains both polar and non-polar amino acid, making the protein <scene name='93/934003/Amphipathic/1'>amphipathic</scene>. The MBD enzymes is noted to have evolved from the ATP-depedent PMD enzyme where it lost its ability to bind to kinase and became ATP-indepedent. This belief is supported by the discovery that the MBD enzyme's ligand binding site overlaps with the ATP binding site observed in its homologous enzyme, DMD.