RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/19141282http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19141282http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19141282http://www.w3.org/2000/01/rdf-schema#comment"IL-7 and IL-7Ralpha bind the gamma(c) receptor, forming a complex crucial to several signaling cascades leading to the development and homeostasis of T and B cells. We report that the IL-7Ralpha ectodomain uses glycosylation to modulate its binding constants to IL-7, unlike the other receptors in the gamma(c) family. IL-7 binds glycosylated IL-7Ralpha 300-fold more tightly than unglycosylated IL-7Ralpha, and the enhanced affinity is attributed primarily to an accelerated on rate. Structural comparison of IL-7 in complex to both forms of IL-7Ralpha reveals that glycosylation does not participate directly in the binding interface. The SCID mutations of IL-7Ralpha locate outside the binding interface with IL-7, suggesting that the expressed mutations cause protein folding defects in IL-7Ralpha. The IL-7/IL-7Ralpha structures provide a window into the molecular recognition events of the IL-7 signaling cascade and provide sites to target for designing new therapeutics to treat IL-7-related diseases."xsd:string
http://purl.uniprot.org/citations/19141282http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2008.10.019"xsd:string
http://purl.uniprot.org/citations/19141282http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2008.10.019"xsd:string
http://purl.uniprot.org/citations/19141282http://purl.uniprot.org/core/author"McElroy C.A."xsd:string
http://purl.uniprot.org/citations/19141282http://purl.uniprot.org/core/author"McElroy C.A."xsd:string
http://purl.uniprot.org/citations/19141282http://purl.uniprot.org/core/author"Walsh S.T."xsd:string
http://purl.uniprot.org/citations/19141282http://purl.uniprot.org/core/author"Walsh S.T."xsd:string
http://purl.uniprot.org/citations/19141282http://purl.uniprot.org/core/author"Dohm J.A."xsd:string
http://purl.uniprot.org/citations/19141282http://purl.uniprot.org/core/author"Dohm J.A."xsd:string
http://purl.uniprot.org/citations/19141282http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19141282http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19141282http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/19141282http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/19141282http://purl.uniprot.org/core/pages"54-65"xsd:string
http://purl.uniprot.org/citations/19141282http://purl.uniprot.org/core/pages"54-65"xsd:string
http://purl.uniprot.org/citations/19141282http://purl.uniprot.org/core/title"Structural and biophysical studies of the human IL-7/IL-7Ralpha complex."xsd:string
http://purl.uniprot.org/citations/19141282http://purl.uniprot.org/core/title"Structural and biophysical studies of the human IL-7/IL-7Ralpha complex."xsd:string
http://purl.uniprot.org/citations/19141282http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/19141282http://purl.uniprot.org/core/volume"17"xsd:string
http://purl.uniprot.org/citations/19141282http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19141282
http://purl.uniprot.org/citations/19141282http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19141282
http://purl.uniprot.org/citations/19141282http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19141282
http://purl.uniprot.org/citations/19141282http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19141282