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http://purl.uniprot.org/citations/14634014http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14634014http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/14634014http://www.w3.org/2000/01/rdf-schema#comment"Echovirus type 12 (EV12), an Enterovirus of the Picornaviridae family, uses the complement regulator decay-accelerating factor (DAF, CD55) as a cellular receptor. We have calculated a three-dimensional reconstruction of EV12 bound to a fragment of DAF consisting of short consensus repeat domains 3 and 4 from cryo-negative stain electron microscopy data (EMD code 1057). This shows that, as for an earlier reconstruction of the related echovirus type 7 bound to DAF, attachment is not within the viral canyon but occurs close to the 2-fold symmetry axes. Despite this general similarity our reconstruction reveals a receptor interaction that is quite different from that observed for EV7. Fitting of the crystallographic co-ordinates for DAF(34) and EV11 into the reconstruction shows a close agreement between the crystal structure of the receptor fragment and the density for the virus-bound receptor, allowing unambiguous positioning of the receptor with respect to the virion (PDB code 1UPN). Our finding that the mode of virus-receptor interaction in EV12 is distinct from that seen for EV7 raises interesting questions regarding the evolution and biological significance of the DAF binding phenotype in these viruses."xsd:string
http://purl.uniprot.org/citations/14634014http://purl.org/dc/terms/identifier"doi:10.1074/jbc.M311334200"xsd:string
http://purl.uniprot.org/citations/14634014http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m311334200"xsd:string
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/author"Bhella D."xsd:string
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/author"Bhella D."xsd:string
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/author"Chaudhry Y."xsd:string
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/author"Chaudhry Y."xsd:string
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/author"Goodfellow I.G."xsd:string
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/author"Goodfellow I.G."xsd:string
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/author"Roversi P."xsd:string
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/author"Roversi P."xsd:string
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/author"Lea S.M."xsd:string
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/author"Lea S.M."xsd:string
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/author"Evans D.J."xsd:string
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/author"Evans D.J."xsd:string
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/author"Pettigrew D."xsd:string
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/author"Pettigrew D."xsd:string
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/pages"8325-8332"xsd:string
http://purl.uniprot.org/citations/14634014http://purl.uniprot.org/core/pages"8325-8332"xsd:string