3c2i: Difference between revisions

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~~'''~~The Crystal Structure of Methyl-CpG Binding Domain of Human MeCP2 in Complex with a Methylated DNA Sequence from BDNF~~'''~~

===The Crystal Structure of Methyl-CpG Binding Domain of Human MeCP2 in Complex with a Methylated DNA Sequence from BDNF===

~~==Overview==~~

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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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_18313390}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 18313390 is the PubMed ID number.

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==Disease==

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[[Category: Transcription regulator]]

[[Category: Water mediated recognition]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed May 14 11~~:31:36 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:37:43 2008''

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-[[Image:3c2i.jpg|left|200px]]
+{{Seed}}
+[[Image:3c2i.png|left|200px]]
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 {{STRUCTURE_3c2i|  PDB=3c2i  |  SCENE=  }}
-'''The Crystal Structure of Methyl-CpG Binding Domain of Human MeCP2 in Complex with a Methylated DNA Sequence from BDNF'''
+===The Crystal Structure of Methyl-CpG Binding Domain of Human MeCP2 in Complex with a Methylated DNA Sequence from BDNF===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_18313390}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18313390 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18313390}}
 ==Disease==
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 [[Category: Transcription regulator]]
 [[Category: Water mediated recognition]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 14 11:31:36 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:37:43 2008''