The solution structure of the domain from MeCP2 that binds to methylated DNA.

@article{Wakefield1999TheSS,
  title={The solution structure of the domain from MeCP2 that binds to methylated DNA.},
  author={Robert I D Wakefield and Brian O Smith and Xinsheng Nan and Andrew Free and Andreas Soteriou and Du{\vs}an Uhr{\'i}n and Adrian Bird and Paul N. Barlow},
  journal={Journal of molecular biology},
  year={1999},
  volume={291 5},
  pages={1055-65}
}
MeCP2 is an abundant mammalian protein that binds methylated CpG (mCpG) sequences within double-stranded DNA, represses transcription by recruiting histone deacetylases, and is essential for embryonic development. It is one of a family of proteins which mediate the biological consequences of DNA methylation. These proteins each possess a sequence motif of about 70 residues which, in MeCP2, form a domain necessary and sufficient for binding to mCpG. The solution structure of the mCpG-binding… CONTINUE READING
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