View source for Methyl CpG binding protein

<StructureSection load='4evv' size='350' side='right' caption='Structure of mouse MBD4 glycosylate domain complex with DNA containing mismatch, ethylene glycol and Ni+2 ion (green)  (PDB code [[4evv]]).' scene='59/597003/Cv/1'>

== Function ==

'''Methyl CpG binding proteins''' are called MBD1 to MBD4 and contain a methyl-CpG binding domain (MBD) which binds to methylated DNA<ref>PMID:11746232</ref>.<br />
•	'''MBD1''' is a transcription regulator.  It reverts methylated cytosine bases to cytosine.<br />
•	'''MBD2''' is part of the MeCP1 complex which contains also NuRD.  MBD2 recruits histone deacetylases and DNA methyltransferases.  MBD2 functions as a scaffold protein promoting repression.<br />
•	'''MBD3''' binds to hydroxymethylated DNA.<br />
•	'''MBD4''' has a G:T mispair-specific activity.<br />
•	'''Methyl CpG binding protein 2''' (MeCP2) is present in mature nerve cells and is involved in turning off several genes. For more details see [[Methyl CpG Binding Protein 2]] and [[Rett Syndrome Protein]].<br />

== Disease ==
Mutations in MBD2 are involved in Rett syndrome<ref>PMID:11738862</ref>.

== Relevance ==
MBD1 has a role in lung, prostate, pancreatic, colorectal cancers and promyelocytic leukemia. MBD2 has a role in lung, prostate, renal, colorectal cancers.  MBD3 has a role in lung, prostate, ovarian cancers and promyelocytic leukemia.  MBD4 has a role in gastric, liver and colorectal cancers.

== Structural highlights ==
<scene name='59/597003/Cv/3'>Thymine from the mismatched G:T pair flips out from the DNA strand and interchelates with MBD4 residues Lys and Leu</scene><ref>PMID:22740654</ref>.

==3D structures of methyl CpG binding protein==
[[Methyl CpG binding protein 3D structures]]

</StructureSection>

== References ==
<references/>

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