Methyl CpG binding protein

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== Structural highlights ==
== Structural highlights ==
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<scene name='59/597003/Cv/2'>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>.
+
<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>.
</StructureSection>
</StructureSection>

Revision as of 13:45, 11 July 2019

Structure of mouse MBD4 glycosylate domain complex with DNA containing mismatch, ethylene glycol and Ni+2 ion (green) (PDB code 4evv).

Drag the structure with the mouse to rotate

3D structures of methyl CpG binding protein

Updated on 11-July-2019

References

  1. Wade PA. Methyl CpG-binding proteins and transcriptional repression. Bioessays. 2001 Dec;23(12):1131-7. PMID:11746232 doi:http://dx.doi.org/10.1002/bies.10008
  2. Van den Veyver IB, Zoghbi HY. Mutations in the gene encoding methyl-CpG-binding protein 2 cause Rett syndrome. Brain Dev. 2001 Dec;23 Suppl 1:S147-51. PMID:11738862
  3. Hashimoto H, Zhang X, Cheng X. Excision of thymine and 5-hydroxymethyluracil by the MBD4 DNA glycosylase domain: structural basis and implications for active DNA demethylation. Nucleic Acids Res. 2012 Jun 27. PMID:22740654 doi:10.1093/nar/gks628

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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