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. |