1IG4

Solution Structure of the Methyl-CpG-Binding Domain of Human MBD1 in Complex with Methylated DNA

Summary for 1IG4

• Entry DOI: 10.2210/pdb1ig4/pdb
• Descriptor: 5'-D(*GP*TP*AP*TP*CP*(5CM)P*GP*GP*AP*TP*AP*C)-3', Methyl-CpG Binding Protein (2 entities in total)
• Functional Keywords: protein-dna complex, alpha-beta, double helix, recognition via beta-sheet, transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus speckle: Q9UIS9
• Total number of polymer chains: 3
• Total formula weight: 15869.61

Authors

Ohki, I.,Shimotake, N.,Fujita, N.,Jee, J.-G.,Ikegami, T.,Nakao, M.,Shirakawa, M. (deposition date: 2001-04-17, release date: 2001-05-30, Last modification date: 2024-05-22)

Primary citation

Ohki, I.,Shimotake, N.,Fujita, N.,Jee, J.,Ikegami, T.,Nakao, M.,Shirakawa, M.
Solution structure of the methyl-CpG binding domain of human MBD1 in complex with methylated DNA.
Cell(Cambridge,Mass.), 105:487-497, 2001

PubMed Abstract: 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.

PubMed: 11371345
DOI: 10.1016/S0092-8674(01)00324-5

Experimental method

SOLUTION NMR