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http://purl.uniprot.org/citations/12086624http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12086624http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12086624http://www.w3.org/2000/01/rdf-schema#comment"Rotaviruses, segmented double-stranded RNA viruses, co-opt the eukaryotic translation machinery with the aid of nonstructural protein 3 (NSP3), a rotaviral functional homolog of the cellular poly(A) binding protein (PABP). NSP3 binds to viral mRNA 3' consensus sequences and circularizes mRNA via interactions with eIF4G. Here, we present the X-ray structure of the C-terminal domain of NSP3 (NSP3-C) recognizing a fragment of eIF4GI. Homodimerization of NSP3-C yields a symmetric, elongated, largely alpha-helical structure with two hydrophobic eIF4G binding pockets at the dimer interface. Site-directed mutagenesis and isothermal titration calorimetry documented that NSP3 and PABP use analogous eIF4G recognition strategies, despite marked differences in tertiary structure."xsd:string
http://purl.uniprot.org/citations/12086624http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(02)00555-5"xsd:string
http://purl.uniprot.org/citations/12086624http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(02)00555-5"xsd:string
http://purl.uniprot.org/citations/12086624http://purl.uniprot.org/core/author"Burley S.K."xsd:string
http://purl.uniprot.org/citations/12086624http://purl.uniprot.org/core/author"Burley S.K."xsd:string
http://purl.uniprot.org/citations/12086624http://purl.uniprot.org/core/author"Groft C.M."xsd:string
http://purl.uniprot.org/citations/12086624http://purl.uniprot.org/core/author"Groft C.M."xsd:string
http://purl.uniprot.org/citations/12086624http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12086624http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12086624http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/12086624http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/12086624http://purl.uniprot.org/core/pages"1273-1283"xsd:string
http://purl.uniprot.org/citations/12086624http://purl.uniprot.org/core/pages"1273-1283"xsd:string
http://purl.uniprot.org/citations/12086624http://purl.uniprot.org/core/title"Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization."xsd:string
http://purl.uniprot.org/citations/12086624http://purl.uniprot.org/core/title"Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization."xsd:string
http://purl.uniprot.org/citations/12086624http://purl.uniprot.org/core/volume"9"xsd:string
http://purl.uniprot.org/citations/12086624http://purl.uniprot.org/core/volume"9"xsd:string
http://purl.uniprot.org/citations/12086624http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12086624
http://purl.uniprot.org/citations/12086624http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12086624
http://purl.uniprot.org/citations/12086624http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12086624
http://purl.uniprot.org/citations/12086624http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12086624
http://purl.uniprot.org/uniprot/Q04637http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12086624
http://purl.uniprot.org/uniprot/P03536http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/12086624