http://purl.uniprot.org/citations/15837194 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15837194 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15837194 | http://www.w3.org/2000/01/rdf-schema#comment | "Human IL-10 (hIL-10) is a cytokine that modulates diverse immune responses. The Epstein-Barr virus (EBV) genome contains an IL-10 homolog (vIL-10) that shares high sequence and structural similarity with hIL-10. Although vIL-10 suppresses inflammatory responses like hIL-10, it cannot activate many other immunostimulatory functions performed by the cellular cytokine. These functional differences have been correlated with the approximately 1000-fold lower affinity of vIL-10, compared to hIL-10, for the IL-10R1 receptor chain. To define the structural basis for these observations, crystal structures of vIL-10 and a vIL-10 point mutant were determined bound to the soluble IL-10R1 receptor fragment (sIL-10R1) at 2.8 and 2.7 A resolution, respectively. The structures reveal that subtle changes in the conformation and dynamics of the vIL-10 AB and CD loops and an orientation change of vIL-10 on sIL-10R1 are the main factors responsible for vIL-10's reduced affinity for sIL-10R1 and its distinct biological profile."xsd:string |
http://purl.uniprot.org/citations/15837194 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.str.2005.01.016"xsd:string |
http://purl.uniprot.org/citations/15837194 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.str.2005.01.016"xsd:string |
http://purl.uniprot.org/citations/15837194 | http://purl.uniprot.org/core/author | "Jones B.C."xsd:string |
http://purl.uniprot.org/citations/15837194 | http://purl.uniprot.org/core/author | "Jones B.C."xsd:string |
http://purl.uniprot.org/citations/15837194 | http://purl.uniprot.org/core/author | "Logsdon N.J."xsd:string |
http://purl.uniprot.org/citations/15837194 | http://purl.uniprot.org/core/author | "Logsdon N.J."xsd:string |
http://purl.uniprot.org/citations/15837194 | http://purl.uniprot.org/core/author | "Walter M.R."xsd:string |
http://purl.uniprot.org/citations/15837194 | http://purl.uniprot.org/core/author | "Walter M.R."xsd:string |
http://purl.uniprot.org/citations/15837194 | http://purl.uniprot.org/core/author | "Yoon S.I."xsd:string |
http://purl.uniprot.org/citations/15837194 | http://purl.uniprot.org/core/author | "Yoon S.I."xsd:string |
http://purl.uniprot.org/citations/15837194 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/15837194 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
http://purl.uniprot.org/citations/15837194 | http://purl.uniprot.org/core/name | "Structure"xsd:string |
http://purl.uniprot.org/citations/15837194 | http://purl.uniprot.org/core/name | "Structure"xsd:string |
http://purl.uniprot.org/citations/15837194 | http://purl.uniprot.org/core/pages | "551-564"xsd:string |
http://purl.uniprot.org/citations/15837194 | http://purl.uniprot.org/core/pages | "551-564"xsd:string |
http://purl.uniprot.org/citations/15837194 | http://purl.uniprot.org/core/title | "Same structure, different function crystal structure of the Epstein-Barr virus IL-10 bound to the soluble IL-10R1 chain."xsd:string |
http://purl.uniprot.org/citations/15837194 | http://purl.uniprot.org/core/title | "Same structure, different function crystal structure of the Epstein-Barr virus IL-10 bound to the soluble IL-10R1 chain."xsd:string |
http://purl.uniprot.org/citations/15837194 | http://purl.uniprot.org/core/volume | "13"xsd:string |
http://purl.uniprot.org/citations/15837194 | http://purl.uniprot.org/core/volume | "13"xsd:string |
http://purl.uniprot.org/citations/15837194 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15837194 |
http://purl.uniprot.org/citations/15837194 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15837194 |