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1ig4
From Proteopedia
(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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| - | [[Image:1ig4.gif|left|200px]]<br /> | + | [[Image:1ig4.gif|left|200px]]<br /><applet load="1ig4" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ig4" size=" | + | |
caption="1ig4" /> | caption="1ig4" /> | ||
'''Solution Structure of the Methyl-CpG-Binding Domain of Human MBD1 in Complex with Methylated DNA'''<br /> | '''Solution Structure of the Methyl-CpG-Binding Domain of Human MBD1 in Complex with Methylated DNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In vertebrates, the biological consequences of DNA methylation are often | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IG4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1IG4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IG4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Fujita, N.]] | [[Category: Fujita, N.]] | ||
[[Category: Ikegami, T.]] | [[Category: Ikegami, T.]] | ||
| - | [[Category: Jee, J | + | [[Category: Jee, J G.]] |
[[Category: Nakao, M.]] | [[Category: Nakao, M.]] | ||
[[Category: Ohki, I.]] | [[Category: Ohki, I.]] | ||
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[[Category: recognition via beta-sheet]] | [[Category: recognition via beta-sheet]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:29 2008'' |
Revision as of 11:11, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 13:11:29 2008
