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http://purl.uniprot.org/citations/12093920http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12093920http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12093920http://www.w3.org/2000/01/rdf-schema#comment"Human IL-10 (hIL-10) modulates critical immune and inflammatory responses by way of interactions with its high-(IL-10R1) and low-affinity (IL-10R2) cell surface receptors. Human cytomegalovirus exploits the IL-10 signaling pathway by expressing a functional viral IL-10 homolog (cmvIL-10), which shares only 27% sequence identity with hIL-10 yet signals through IL-10R1 and IL-10R2. To define the molecular basis of this virus-host interaction, we determined the 2.7-A crystal structure of cmvIL-10 bound to the extracellular fragment of IL-10R1 (sIL-10R1). The structure reveals cmvIL-10 forms a disulfide-linked homodimer that binds two sIL-10R1 molecules. Although cmvIL-10 and hIL-10 share similar intertwined topologies and sIL-10R1 binding sites, their respective interdomain angles differ by approximately 40 degrees. This difference results in a striking re-organization of the IL-10R1s in the putative cell surface complex. Solution binding studies show cmvIL-10 and hIL-10 share essentially identical affinities for sIL-10R1 whereas the Epstein-Barr virus IL-10 homolog (ebvIL-10), whose structure is highly similar to hIL-10, exhibits a approximately 20-fold reduction in sIL-10R1 affinity. Our results suggest cmvIL-10 and ebvIL-10 have evolved different molecular mechanisms to engage the IL-10 receptors that ultimately enhance the respective ability of their virus to escape immune detection."xsd:string
http://purl.uniprot.org/citations/12093920http://purl.org/dc/terms/identifier"doi:10.1073/pnas.152147499"xsd:string
http://purl.uniprot.org/citations/12093920http://purl.org/dc/terms/identifier"doi:10.1073/pnas.152147499"xsd:string
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/author"Barry P.A."xsd:string
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/author"Barry P.A."xsd:string
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/author"Cook J."xsd:string
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/author"Cook J."xsd:string
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/author"Jones B.C."xsd:string
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/author"Jones B.C."xsd:string
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/author"Josephson K."xsd:string
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/author"Josephson K."xsd:string
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/author"Logsdon N.J."xsd:string
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/author"Logsdon N.J."xsd:string
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/author"Walter M.R."xsd:string
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/author"Walter M.R."xsd:string
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/pages"9404-9409"xsd:string
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/pages"9404-9409"xsd:string
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/title"Crystal structure of human cytomegalovirus IL-10 bound to soluble human IL-10R1."xsd:string
http://purl.uniprot.org/citations/12093920http://purl.uniprot.org/core/title"Crystal structure of human cytomegalovirus IL-10 bound to soluble human IL-10R1."xsd:string