| http://purl.uniprot.org/citations/11485736 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11485736 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11485736 | http://www.w3.org/2000/01/rdf-schema#comment | "Interleukin 10 (IL-10) is a dimeric cytokine that plays a central role in suppressing inflammatory responses. These activities are dependent on the interaction of IL-10 with its high-affinity receptor (IL-10R1). This intermediate complex must subsequently recruit the low-affinity IL-10R2 chain before cell signaling can occur. Here we report the 2.9 A crystal structure of IL-10 bound to a soluble form of IL-10R1 (sIL-10R1). The complex consists of two IL-10s and four sIL-10R1 molecules. Several residues in the IL-10/sIL-10R1 interface are conserved in all IL-10 homologs and their receptors. The data suggests that formation of the active IL-10 signaling complex occurs by a novel molecular recognition paradigm where IL-10R1 and IL-10R2 both recognize the same binding site on IL-10."xsd:string |
| http://purl.uniprot.org/citations/11485736 | http://purl.org/dc/terms/identifier | "doi:10.1016/s1074-7613(01)00169-8"xsd:string |
| http://purl.uniprot.org/citations/11485736 | http://purl.org/dc/terms/identifier | "doi:10.1016/s1074-7613(01)00169-8"xsd:string |
| http://purl.uniprot.org/citations/11485736 | http://purl.uniprot.org/core/author | "Josephson K."xsd:string |
| http://purl.uniprot.org/citations/11485736 | http://purl.uniprot.org/core/author | "Josephson K."xsd:string |
| http://purl.uniprot.org/citations/11485736 | http://purl.uniprot.org/core/author | "Logsdon N.J."xsd:string |
| http://purl.uniprot.org/citations/11485736 | http://purl.uniprot.org/core/author | "Logsdon N.J."xsd:string |
| http://purl.uniprot.org/citations/11485736 | http://purl.uniprot.org/core/author | "Walter M.R."xsd:string |
| http://purl.uniprot.org/citations/11485736 | http://purl.uniprot.org/core/author | "Walter M.R."xsd:string |
| http://purl.uniprot.org/citations/11485736 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11485736 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11485736 | http://purl.uniprot.org/core/name | "Immunity"xsd:string |
| http://purl.uniprot.org/citations/11485736 | http://purl.uniprot.org/core/name | "Immunity"xsd:string |
| http://purl.uniprot.org/citations/11485736 | http://purl.uniprot.org/core/pages | "35-46"xsd:string |
| http://purl.uniprot.org/citations/11485736 | http://purl.uniprot.org/core/pages | "35-46"xsd:string |
| http://purl.uniprot.org/citations/11485736 | http://purl.uniprot.org/core/title | "Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor binding site."xsd:string |
| http://purl.uniprot.org/citations/11485736 | http://purl.uniprot.org/core/title | "Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor binding site."xsd:string |
| http://purl.uniprot.org/citations/11485736 | http://purl.uniprot.org/core/volume | "15"xsd:string |
| http://purl.uniprot.org/citations/11485736 | http://purl.uniprot.org/core/volume | "15"xsd:string |
| http://purl.uniprot.org/citations/11485736 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11485736 |
| http://purl.uniprot.org/citations/11485736 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11485736 |
| http://purl.uniprot.org/citations/11485736 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11485736 |
| http://purl.uniprot.org/citations/11485736 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/11485736 |