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MeCP2 binding to DNA depends upon hydration at methyl-CpG.

Abstract：

:MeCP2 is an essential transcriptional repressor that mediates gene silencing through binding to methylated DNA. Binding specificity has been thought to depend on hydrophobic interactions between cytosine methyl groups and a hydrophobic patch within the methyl-CpG-binding domain (MBD). X-ray analysis of a methylated DNA-MBD cocrystal reveals, however, that the methyl groups make contact with a predominantly hydrophilic surface that includes tightly bound water molecules. This suggests that MeCP2 recognizes hydration of the major groove of methylated DNA rather than cytosine methylation per se. The MeCP2-DNA complex also identifies a unique structural role for T158, the residue most commonly mutated in Rett syndrome.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Ho KL,McNae IW,Schmiedeberg L,Klose RJ,Bird AP,Walkinshaw MD

doi

10.1016/j.molcel.2007.12.028

subject

Has Abstract

pub_date

2008-02-29 00:00:00

pages

525-31

issue

4

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(08)00096-8

journal_volume

29

pub_type

杂志文章

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