| http://purl.uniprot.org/citations/29317535 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/29317535 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/29317535 | http://www.w3.org/2000/01/rdf-schema#comment | "Cytokine signaling through the JAK/STAT pathway controls multiple cellular responses including growth, survival, differentiation, and pathogen resistance. An expansion in the gene regulatory repertoire controlled by JAK/STAT signaling occurs through the interaction of STATs with IRF transcription factors to form ISGF3, a complex that contains STAT1, STAT2, and IRF9 and regulates expression of IFN-stimulated genes. ISGF3 function depends on selective interaction between IRF9, through its IRF-association domain (IAD), with the coiled-coil domain (CCD) of STAT2. Here, we report the crystal structures of the IRF9-IAD alone and in a complex with STAT2-CCD. Despite similarity in the overall structure among respective paralogs, the surface features of the IRF9-IAD and STAT2-CCD have diverged to enable specific interaction between these family members. We derive a model for the ISGF3 complex bound to an ISRE DNA element and demonstrate that the observed interface between STAT2 and IRF9 is required for ISGF3 function in cells."xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1718426115"xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.1718426115"xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/author | "Devos J.M."xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/author | "Devos J.M."xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/author | "Grandvaux N."xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/author | "Grandvaux N."xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/author | "Panne D."xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/author | "Panne D."xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/author | "Rengachari S."xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/author | "Rengachari S."xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/author | "Caron E."xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/author | "Caron E."xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/author | "Groiss S."xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/author | "Groiss S."xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/date | "2018"xsd:gYear |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/date | "2018"xsd:gYear |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/name | "Proc Natl Acad Sci U S A"xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/pages | "E601-E609"xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/pages | "E601-E609"xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/title | "Structural basis of STAT2 recognition by IRF9 reveals molecular insights into ISGF3 function."xsd:string |
| http://purl.uniprot.org/citations/29317535 | http://purl.uniprot.org/core/title | "Structural basis of STAT2 recognition by IRF9 reveals molecular insights into ISGF3 function."xsd:string |