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http://purl.uniprot.org/citations/23936039http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23936039http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23936039http://www.w3.org/2000/01/rdf-schema#comment"Human paternally expressed gene 3 protein (PEG3) is a large multi-domain entity with diverse biological functions, including acting as a transcription factor. PEG3 contains twelve Cys2-His2 type zinc finger domains, extended regions of predicted disorder and at the N-terminus a SCAN domain. PEG3 has been identified as partner of the E3 ubiquitin-protein ligase Siah1, an association we sought to investigate. An efficient bacterial recombinant expression system of the human PEG3-SCAN domain was prepared and crystals appeared spontaneously when the protein was being concentrated after purification. The structure was determined at 1.95 Å resolution and reveals a polypeptide fold of five helices in an extended configuration. An extensive dimerization interface, using almost a quarter of the solvent accessible surface, and key salt bridge interactions explain the stability of the dimer. Comparison with other SCAN domains reveals a high degree of conservation involving residues that contribute to the dimer interface. The PEG3-SCAN domain appears to constitute an assembly block, enabling PEG3 homo- or heterodimerization to control gene expression in a combinatorial fashion."xsd:string
http://purl.uniprot.org/citations/23936039http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0069538"xsd:string
http://purl.uniprot.org/citations/23936039http://purl.org/dc/terms/identifier"doi:10.1371/journal.pone.0069538"xsd:string
http://purl.uniprot.org/citations/23936039http://purl.uniprot.org/core/author"Hunter W.N."xsd:string
http://purl.uniprot.org/citations/23936039http://purl.uniprot.org/core/author"Hunter W.N."xsd:string
http://purl.uniprot.org/citations/23936039http://purl.uniprot.org/core/author"Eadsforth T.C."xsd:string
http://purl.uniprot.org/citations/23936039http://purl.uniprot.org/core/author"Eadsforth T.C."xsd:string
http://purl.uniprot.org/citations/23936039http://purl.uniprot.org/core/author"Rimsa V."xsd:string
http://purl.uniprot.org/citations/23936039http://purl.uniprot.org/core/author"Rimsa V."xsd:string
http://purl.uniprot.org/citations/23936039http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23936039http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23936039http://purl.uniprot.org/core/name"PLoS ONE"xsd:string
http://purl.uniprot.org/citations/23936039http://purl.uniprot.org/core/name"PLoS ONE"xsd:string
http://purl.uniprot.org/citations/23936039http://purl.uniprot.org/core/pages"E69538"xsd:string
http://purl.uniprot.org/citations/23936039http://purl.uniprot.org/core/pages"E69538"xsd:string
http://purl.uniprot.org/citations/23936039http://purl.uniprot.org/core/title"Structure of the SCAN domain of human paternally expressed gene 3 protein."xsd:string
http://purl.uniprot.org/citations/23936039http://purl.uniprot.org/core/title"Structure of the SCAN domain of human paternally expressed gene 3 protein."xsd:string
http://purl.uniprot.org/citations/23936039http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/23936039http://purl.uniprot.org/core/volume"8"xsd:string
http://purl.uniprot.org/citations/23936039http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23936039
http://purl.uniprot.org/citations/23936039http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/23936039
http://purl.uniprot.org/citations/23936039http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23936039
http://purl.uniprot.org/citations/23936039http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/23936039