Structural basis of STAT2 recognition by IRF9 reveals molecular insights into ISGF3 function.

Cytokine signaling through the pathway controls multiple cellular responses including growth, survival, differentiation, and pathogen resistance. An expansion in the gene regulatory repertoire controlled by JAK/duanyu1813 signaling occurs through the interaction of with IRF transcription factors to form ISGF3, a complex that contains 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 Here, we report the crystal structures of the IRF9-IAD alone and in a complex with Despite similarity in the overall structure among respective paralogs, the surface features of the IRF9-IAD and 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 and IRF9 is required for ISGF3 function in cells.

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