Methyl-CpG DNA binding
IPR001739
Definition
This entry represents the MBD domain. The MBD folds into an α/β-sandwich structure comprising a layer of twisted β-sheet, backed by another layer formed by the α1 helix and a hairpin loop at the C-terminal. These layers are amphipathic, with the α1 helix and the β-sheet lying parallel and the hydrophobic faces tightly packed against each other. The β-sheet is composed of two long inner strands (β2 and β3) sandwiched by two shorter outer strands (β1 and β4) PMID:11371345. Methylation at CpG dinucleotide, the most common DNA modification in eukaryotes, has been correlated with gene silencing associated with various phenomena such as genomic imprinting, transposon and chromosome X inactivation, differentiation, and cancer. Effects of DNA methylation are mediated through proteins which bind to symmetrically methylated CpGs. Such proteins contain a specific domain of ~70 residues, the methyl-CpG-binding domain (MBD), which is linked to additional domains associated with chromatin, such as the bromodomain, the AT hook motif, the SET domain, or the PHD finger. MBD-containing proteins appear to act as structural proteins, which recruit a variety of histone deacetylase (HDAC) complexes and chromatin remodelling factors, leading to chromatin compaction and, consequently, to transcriptional repression. The MBD of MeCP2, MBD1, MBD2, MBD4 and BAZ2 mediates binding to DNA, in case of MeCP2, MBD1 and MBD2 preferentially to methylated CpG. In case of human MBD3 and SETDB1 the MBD has been shown to mediate protein-protein interactions [[cite:PMID:12529184], [cite:PMID:12787239]].
11 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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