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http://purl.uniprot.org/citations/32187518http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32187518http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/32187518http://www.w3.org/2000/01/rdf-schema#comment"Interleukin-17A (IL-17A), IL-17F, and IL-17A/F heterodimers are key cytokines of the innate and adaptive immune response. Dysregulation of the IL-17 pathway contributes to immune pathology, and it is therefore important to elucidate the molecular mechanisms that govern IL-17 recognition and signaling. The receptor IL-17RC is thought to act in concert with IL-17RA to transduce IL-17A-, IL-17F-, and IL-17A/F-mediated signals. We report the crystal structure of the extracellular domain of human IL-17RC in complex with IL-17F. In contrast to the expected model, we found that IL-17RC formed a symmetrical 2:1 complex with IL-17F, thus competing with IL-17RA for cytokine binding. Using biophysical techniques, we showed that IL-17A and IL-17A/F also form 2:1 complexes with IL-17RC, suggesting the possibility of IL-17RA-independent IL-17 signaling pathways. The crystal structure of the IL-17RC:IL-17F complex provides a structural basis for IL-17F signaling through IL-17RC, with potential therapeutic applications for respiratory allergy and inflammatory bowel diseases."xsd:string
http://purl.uniprot.org/citations/32187518http://purl.org/dc/terms/identifier"doi:10.1016/j.immuni.2020.02.004"xsd:string
http://purl.uniprot.org/citations/32187518http://purl.org/dc/terms/identifier"doi:10.1016/j.immuni.2020.02.004"xsd:string
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/author"Goepfert A."xsd:string
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/author"Goepfert A."xsd:string
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/author"Blank J."xsd:string
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/author"Blank J."xsd:string
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/author"Kolbinger F."xsd:string
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/author"Kolbinger F."xsd:string
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/author"Lehmann S."xsd:string
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/author"Lehmann S."xsd:string
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/author"Rondeau J.M."xsd:string
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/author"Rondeau J.M."xsd:string
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/date"2020"xsd:gYear
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/name"Immunity"xsd:string
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/name"Immunity"xsd:string
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/pages"499-512.e5"xsd:string
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/pages"499-512.e5"xsd:string
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/title"Structural Analysis Reveals that the Cytokine IL-17F Forms a Homodimeric Complex with Receptor IL-17RC to Drive IL-17RA-Independent Signaling."xsd:string
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/title"Structural Analysis Reveals that the Cytokine IL-17F Forms a Homodimeric Complex with Receptor IL-17RC to Drive IL-17RA-Independent Signaling."xsd:string
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/volume"52"xsd:string
http://purl.uniprot.org/citations/32187518http://purl.uniprot.org/core/volume"52"xsd:string