1QWT

Auto-inhibitory interferon regulation factor-3 (IRF3) transactivation domain

Summary for 1QWT

• Entry DOI: 10.2210/pdb1qwt/pdb
• Descriptor: Interferon regulatory factor 3, PHOSPHATE ION (3 entities in total)
• Functional Keywords: dna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q14653
• Total number of polymer chains: 2
• Total formula weight: 57079.37

Authors

Qin, B.Y. (deposition date: 2003-09-03, release date: 2003-10-14, Last modification date: 2024-10-30)

Primary citation

Qin, B.Y.,Liu, C.,Lam, S.S.,Srinath, H.,Delston, R.,Correia, J.J.,Derynck, R.,Lin, K.
Crystal structure of IRF-3 reveals mechanism of autoinhibition and virus induced phospho-activation
Nat.Struct.Biol., 10:913-921, 2003

PubMed Abstract: IRF-3, a member of the interferon regulatory factor (IRF) family of transcription factors, functions as a molecular switch for antiviral activity. IRF-3 uses an autoinhibitory mechanism to suppress its transactivation potential in uninfected cells, and virus infection induces phosphorylation and activation of IRF-3 to initiate the antiviral responses. The crystal structure of the IRF-3 transactivation domain reveals a unique autoinhibitory mechanism, whereby the IRF association domain and the flanking autoinhibitory elements condense to form a hydrophobic core. The structure suggests that phosphorylation reorganizes the autoinhibitory elements, leading to unmasking of a hydrophobic active site and realignment of the DNA binding domain for transcriptional activation. IRF-3 exhibits marked structural and surface electrostatic potential similarity to the MH2 domain of the Smad protein family and the FHA domain, suggesting a common molecular mechanism of action among this superfamily of signaling mediators.

PubMed: 14555996
DOI: 10.1038/nsb1002

Experimental method

X-RAY DIFFRACTION (2.1 Å)