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Publication : Solution structure of the methyl-CpG binding domain of human MBD1 in complex with methylated DNA.

First Author  Ohki I Year  2001
Journal  Cell Volume  105
Issue  4 Pages  487-97
PubMed ID  11371345 Mgi Jnum  J:69464
Mgi Id  MGI:1934695 Doi  10.1016/s0092-8674(01)00324-5
Citation  Ohki I, et al. (2001) Solution structure of the methyl-CpG binding domain of human MBD1 in complex with methylated DNA. Cell 105(4):487-97
abstractText  In vertebrates, the biological consequences of DNA methylation are often mediated by protein factors containing conserved methyl-CpG binding domains (MBDs). Mutations in the MBD protein MeCP2 cause the neurodevelopmental disease Rett syndrome. We report here the solution structure of the MBD of the human methylation-dependent transcriptional regulator MBD1 bound to methylated DNA. DNA binding causes a loop in MBD1 to fold into a major and novel DNA binding interface. Recognition of the methyl groups and CG sequence at the methylation site is due to five highly conserved residues that form a hydrophobic patch. The structure indicates how MBD may access nucleosomal DNA without encountering steric interference from core histones, and provides a basis to interpret mutations linked to Rett syndrome in MeCP2.
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