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7JFL

Crystal structure of human phosphorylated IRF-3 bound to CBP

Summary for 7JFL
Entry DOI10.2210/pdb7jfl/pdb
DescriptorInterferon regulatory factor 3, CREB-binding protein (3 entities in total)
Functional Keywordstranscription factor, phosphorylation, innate immunity, immune system
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains4
Total formula weight58090.01
Authors
Li, P.,Jing, T.,Zhao, B. (deposition date: 2020-07-17, release date: 2020-09-09, Last modification date: 2024-11-20)
Primary citationJing, T.,Zhao, B.,Xu, P.,Gao, X.,Chi, L.,Han, H.,Sankaran, B.,Li, P.
The Structural Basis of IRF-3 Activation upon Phosphorylation.
J Immunol., 205:1886-1896, 2020
Cited by
PubMed Abstract: The innate immune system is the first line of defense against bacterial and viral infections. The recognition of pathogen-associated molecular patterns by the RIG-I-like receptors, TLRs, and cGAS leads to the induction of IFN-I by activating the transcription factor IRF-3. Although the mechanism of IRF-3 activation has been extensively studied, the structural basis of IRF-3 activation upon phosphorylation is not fully understood. In this study, we determined the crystal structures of phosphorylated human and mouse IRF-3 bound to CREB-binding protein (CBP), which reveal that phosphorylated IRF-3 forms a dimer via pSer (pSer in mouse IRF-3) and a downstream LIS motif. Size-exclusion chromatography and cell-based studies show that mutations of key residues interacting with pSer severely impair IRF-3 activation and IFN-β induction. By contrast, phosphorylation of Ser within the LIS motif of human IRF-3 only plays a moderate role in IRF-3 activation. The mouse IRF-3/CBP complex structure reveals that the mechanism of mouse IRF-3 activation is similar but distinct from human IRF-3. These structural and functional studies reveal the detailed mechanism of IRF-3 activation upon phosphorylation.
PubMed: 32826280
DOI: 10.4049/jimmunol.2000026
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.68 Å)
Structure validation

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