HTTP 200 OK
Allow: GET, HEAD
Content-Type: application/json
InterPro-Version: 108.0
InterPro-Version-Minor: 0
Vary: Accept
{
"metadata": {
"accession": "PS50982",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "profile",
"member_databases": null,
"integrated": "IPR001739",
"hierarchy": null,
"name": {
"name": "Methyl-CpG-binding domain (MBD) profile",
"short": "MBD"
},
"description": [
{
"text": "<p>Methylation at CpG dinucleotide, the most common DNA modification in\neukaryotes, has been correlated with gene silencing associated with various\nphenomena such as genomic imprinting, transposon and chromosome X\ninactivation, differenciation, and cancer. Effects of DNA methylation are\nmediated through proteins which bind to symmetrically methylated CpGs. Such\nproteins contain a specific domain of ~70 residues, the methyl-CpG-binding\ndomain (MBD), which is linked to additional domains associated with chromatin,\nsuch as the bromodomain, the AT hook motif,the SET domain, or the PHD finger. MBD-containing\nproteins appear to act as structural proteins, which recruit a variety of\nhistone deacetylase (HDAC) complexes and chromatin remodeling factors, leading\nto chromatin compaction and, consequently, to transcriptional repression. The\nMBD of MeCP2, MBD1, MBD2, MBD4 and BAZ2 mediates binding to DNA, in case of\nMeCP2, MBD1 and MBD2 preferentially to methylated CpG. In case of human MBD3\nand SETDB1 the MBD has been shown to mediate protein-protein interactions\n[[cite:PUB00015393]][[cite:PUB00015391]].\n\nThe MBD folds into an alpha/beta sandwich structure comprising a layer of\ntwisted beta sheet, backed by another layer formed by the alpha1 helix and a\nhairpin loop at the C terminus. These layers are both\namphipathic, with the alpha1 helix and the beta sheet lying parallel and the\nhydrophobic faces tighly packed against each other. The beta sheet is composed\nof two long inner strands (beta2 and beta3) sandwiched by two shorter outer\nstrands (beta1 and beta4) [[cite:PUB00015392]].\n\nSome protein known to contain a MBD domain are listed below:\n\n - Vertebrate methyl-CpG binding proteins MBD1, a transcriptional regulator.\n - Vertebrate methyl-CpG binding proteins MBD2.\n - Vertebrate methyl-CpG-binding protein 2 (MeCP-2 protein). It is implicated\n in a human neurological disorder called Rett syndrome. Symptoms of this\n syndrome are mental retardation, loss of speech and purposeful hand use,\n autism, ataxia, and stereotypic hand movements.\n - Vertebrate bromodomain adjacent to zinc finger domain 2A (BAZ2A/TIP5). It\n is part of the NoRC, nucleolar remodeling complex, which represses rDNA\n transcription by recruiting histone methyltransferases, HDACs and DNA\n methyltransferases.\n - Vertebrate bromodomain adjacent to zinc finger domain 2B (BAZ2B).\n - Vertebrate histone-lysine N-methyltransferase, H3 lysine-9 specific 4\n (EC 2.1.1.43) (SETDB1).\n - Vertebrate probable histone-lysine N-methyltransferase, H3 lysine-9\n specific (EC 2.1.1.43) (SETDB2 or CLLD8).\n - Arabidopsis thaliana AtMBD 1-12. No sequence homology is found between\n AtMBDs and mammalian MBDs outside the MBD motif.\n\nThe profile we developed covers the entire MBD domain.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00015392": {
"PMID": 11371345,
"ISBN": null,
"volume": "105",
"issue": "4",
"year": 2001,
"title": "Solution structure of the methyl-CpG binding domain of human MBD1 in complex with methylated DNA.",
"URL": null,
"raw_pages": "487-97",
"medline_journal": "Cell",
"ISO_journal": "Cell",
"authors": [
"Ohki I",
"Shimotake N",
"Fujita N",
"Jee J",
"Ikegami T",
"Nakao M",
"Shirakawa M."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0092-8674(01)00324-5"
},
"PUB00015393": {
"PMID": 12529184,
"ISBN": null,
"volume": "4",
"issue": "1",
"year": 2003,
"title": "Comparative study of methyl-CpG-binding domain proteins.",
"URL": null,
"raw_pages": "1",
"medline_journal": "BMC Genomics",
"ISO_journal": "BMC Genomics",
"authors": [
"Roloff TC",
"Ropers HH",
"Nuber UA."
],
"DOI_URL": "http://dx.doi.org/10.1186/1471-2164-4-1"
},
"PUB00015391": {
"PMID": 12787239,
"ISBN": null,
"volume": "34",
"issue": "5",
"year": 2003,
"title": "Characterization of Arabidopsis thaliana methyl-CpG-binding domain (MBD) proteins.",
"URL": null,
"raw_pages": "565-72",
"medline_journal": "Plant J",
"ISO_journal": "Plant J.",
"authors": [
"Zemach A",
"Grafi G."
],
"DOI_URL": "http://dx.doi.org/10.1046/j.1365-313X.2003.01756.x"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 26035,
"pathways": 0,
"proteins": 24124,
"proteomes": 1694,
"sets": 0,
"structural_models": {
"alphafold": 14527,
"bfvd": 1
},
"structures": 52,
"taxa": 5817
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "3vxv",
"name": "Crystal structure of methyl CpG Binding Domain of MBD4 in complex with the 5mCG/TG sequence"
}
}
}
