1ig4
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(New page: 200px<br /> <applet load="1ig4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ig4" /> '''Solution Structure of the Methyl-CpG-Bindin...)
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Revision as of 15:23, 12 November 2007
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Solution Structure of the Methyl-CpG-Binding Domain of Human MBD1 in Complex with Methylated DNA
Contents |
Overview
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.
Disease
Known disease associated with this structure: Thyroid carcinoma, papillary OMIM:[600299]
About this Structure
1IG4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the methyl-CpG binding domain of human MBD1 in complex with methylated DNA., Ohki I, Shimotake N, Fujita N, Jee J, Ikegami T, Nakao M, Shirakawa M, Cell. 2001 May 18;105(4):487-97. PMID:11371345
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