5OEN

Crystal Structure of STAT2 in complex with IRF9

Summary for 5OEN

• Entry DOI: 10.2210/pdb5oen/pdb
• Descriptor: Interferon regulatory factor 9, Signal transducer and activator of transcription (3 entities in total)
• Functional Keywords: stat2, irf9, transcription
• Biological source: Mus musculus (Mouse); More
• Cellular location: Nucleus: Q61179; Cytoplasm : Q3UDU1
• Total number of polymer chains: 2
• Total formula weight: 39339.13

Authors

Rengachari, S.,Panne, D. (deposition date: 2017-07-09, release date: 2018-01-24, Last modification date: 2024-01-17)

Primary citation

Rengachari, S.,Groiss, S.,Devos, J.M.,Caron, E.,Grandvaux, N.,Panne, D.
Structural basis of STAT2 recognition by IRF9 reveals molecular insights into ISGF3 function.
Proc. Natl. Acad. Sci. U.S.A., 115:E601-E609, 2018

PubMed Abstract: 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.

PubMed: 29317535
DOI: 10.1073/pnas.1718426115

Experimental method

X-RAY DIFFRACTION (2.919 Å)