rdf:type |
|
lifeskim:mentions |
umls-concept:C0012854,
umls-concept:C0037633,
umls-concept:C0086418,
umls-concept:C0439855,
umls-concept:C0678594,
umls-concept:C1148748,
umls-concept:C1382100,
umls-concept:C1417049,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
|
pubmed:issue |
4
|
pubmed:dateCreated |
2001-5-23
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pubmed:databankReference |
|
pubmed: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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pubmed:commentsCorrections |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
May
|
pubmed:issn |
0092-8674
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
18
|
pubmed:volume |
105
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
487-97
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:11371345-Acetylation,
pubmed-meshheading:11371345-Binding Sites,
pubmed-meshheading:11371345-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:11371345-DNA Methylation,
pubmed-meshheading:11371345-DNA-Binding Proteins,
pubmed-meshheading:11371345-Humans,
pubmed-meshheading:11371345-Methyl-CpG-Binding Protein 2,
pubmed-meshheading:11371345-Molecular Sequence Data,
pubmed-meshheading:11371345-Mutagenesis,
pubmed-meshheading:11371345-Protein Structure, Tertiary,
pubmed-meshheading:11371345-Repressor Proteins,
pubmed-meshheading:11371345-Rett Syndrome,
pubmed-meshheading:11371345-Sequence Homology, Amino Acid,
pubmed-meshheading:11371345-Transcription Factors
|
pubmed:year |
2001
|
pubmed:articleTitle |
Solution structure of the methyl-CpG binding domain of human MBD1 in complex with methylated DNA.
|
pubmed:affiliation |
Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, 630-0101, Nara, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|