About: Methyl-CpG-binding domain

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The Methyl-CpG-binding domain (MBD) in molecular biology binds to DNA that contains one or more symmetrically methylated CpGs. MBD has negligible non-specific affinity for unmethylated DNA. In vitro foot-printing with the chromosomal protein MeCP2 showed that the MBD could protect a 12 nucleotide region surrounding a methyl CpG pair. The structure of the MBD domain bound to methylated DNA has been solved (PDB: 3C2I). It recognizes the hydration of the major groove at methylated sites.

Attributes	Values
rdf:type	Thing Biomolecule Biomolecule Protein yago:Abstraction100002137 yago:Family108078020 yago:Group100031264 yago:Organization108008335 yago:YagoLegalActor yago:YagoLegalActorGeo yago:YagoPermanentlyLocatedEntity protein yago:SocialGroup107950920 yago:Unit108189659
rdfs:label	Methyl-CpG-binding domain (en)
rdfs:comment	The Methyl-CpG-binding domain (MBD) in molecular biology binds to DNA that contains one or more symmetrically methylated CpGs. MBD has negligible non-specific affinity for unmethylated DNA. In vitro foot-printing with the chromosomal protein MeCP2 showed that the MBD could protect a 12 nucleotide region surrounding a methyl CpG pair. The structure of the MBD domain bound to methylated DNA has been solved (PDB: 3C2I). It recognizes the hydration of the major groove at methylated sites. (en)
name	MBD (en)
foaf:depiction
dcterms:subject	Protein domains
Wikipage page ID	32752159 (xsd:integer)
Wikipage revision ID	997249374 (xsd:integer)
Link from a Wikipage to another Wikipage	Cancer Amphiphile BAZ2A Protein-protein interaction Proteins MBD1 MBD3 Methylation Homo sapiens Beta sheet DNA Genome Demethylase PHD finger Transposon Bromodomain Transcription (biology) Domain (biology) Helix SET domain Chromatin Binding (molecular) Protein domain Protein folding Protein Protein domains Histone deacetylase CpG site AT-hook Hydrophobic Molecular binding Turn (biochemistry) SETDB1 Molecular biology MBD4 MeCP2 Repressor Chromosome X Secondary structure MBD2
sameAs	Methyl-CpG-binding domain Methyl-CpG-binding domain Methyl-CpG-binding domain
dbp:wikiPageUsesTemplate	dbt:Infobox_protein_family dbt:InterPro_content dbt:Reflist dbt:PDB
thumbnail	wiki-commons:Special:FilePath/Protein_MECP2_PDB_1qk9.png?width=300
SCOP	1 (xsd:integer)
caption	solution structure of human MECO2 (en)
InterPro	IPR001739 (en)
Pfam	PF01429 (en)
Pfam clan	CL0081 (en)
symbol	MBD (en)
has abstract	The Methyl-CpG-binding domain (MBD) in molecular biology binds to DNA that contains one or more symmetrically methylated CpGs. MBD has negligible non-specific affinity for unmethylated DNA. In vitro foot-printing with the chromosomal protein MeCP2 showed that the MBD could protect a 12 nucleotide region surrounding a methyl CpG pair. DNA methylation at CpG dinucleotides, the most common DNA modification in eukaryotes, has been associated with various phenomena such as alterations in chromatin structure, genomic imprinting, transposon and chromosome X inactivation, differentiation, and cancer. Effects of DNA methylation are mediated through proteins that 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, and in cases of MeCP2, MBD1 and MBD2, preferentially to methylated CpG. In human MBD3 and SETDB1, the MBD has been shown to mediate protein-protein interactions. MBDs are also found in DNA demethylase. The MBD folds into an alpha/beta sandwich structure comprising a layer of twisted beta sheet, backed by another layer formed by the alpha1 helix and a hairpin loop at the C terminus. These layers are both amphipathic, with the alpha1 helix and the beta sheet lying parallel and the hydrophobic faces tightly packed against each other. The beta sheet is composed of two long inner strands (beta2 and beta3) sandwiched by two shorter outer strands (beta1 and beta4). The structure of the MBD domain bound to methylated DNA has been solved (PDB: 3C2I). It recognizes the hydration of the major groove at methylated sites. (en)
CDD	cd00122 (en)
prov:wasDerivedFrom	wikipedia-en:Methyl-CpG-binding_domain?oldid=997249374&ns=0
page length (characters) of wiki page	4989 (xsd:nonNegativeInteger)
Symbol	MBD
foaf:isPrimaryTopicOf	wikipedia-en:Methyl-CpG-binding_domain
is Link from a Wikipage to another Wikipage of	Epigenetic regulation of neurogenesis Epigenetics MBD3 DNA methylation Transcription (biology) Transcriptional regulation Transcription factor Biological effects of radiation on the epigenome Methyl cpg binding domain Methyl-CpG-binding domain protein 2 MBD4 Methyl-CpG binding domain
is Wikipage redirect of	Methyl cpg binding domain Methyl-CpG binding domain
is foaf:primaryTopic of	wikipedia-en:Methyl-CpG-binding_domain

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