1J2F

X-ray crystal structure of IRF-3 and its functional implications

Summary for 1J2F

• Entry DOI: 10.2210/pdb1j2f/pdb
• Descriptor: Interferon regulatory factor 3 (2 entities in total)
• Functional Keywords: transcription factor, dna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q14653
• Total number of polymer chains: 2
• Total formula weight: 56758.12

Authors

Takahasi, K.,Noda, N.,Horiuchi, M.,Mori, M.,Okabe, Y.,Fukuhara, Y.,Terasawa, H.,Fujita, T.,Inagaki, F. (deposition date: 2003-01-04, release date: 2003-11-25, Last modification date: 2024-10-30)

Primary citation

Takahasi, K.,Suzuki, N.N.,Horiuchi, M.,Mori, M.,Suhara, W.,Okabe, Y.,Fukuhara, Y.,Terasawa, H.,Akira, S.,Fujita, T.,Inagaki, F.
X-ray crystal structure of IRF-3 and its functional implications.
Nat.Struct.Biol., 10:922-927, 2003

PubMed Abstract: Transcription factor IRF-3 is post-translationally activated by Toll-like receptor (TLR) signaling and has critical roles in the regulation of innate immunity. Here we present the X-ray crystal structure of the C-terminal regulatory domain of IRF-3(175-427) (IRF-3 175C) at a resolution of 2.3 A. IRF-3 175C is structurally similar to the Mad homology domain 2 of the Smad family. Structural and functional analyses reveal phosphorylation-induced IRF-3 dimerization, which generates an extensive acidic pocket responsible for binding with p300/CBP. Although TLR and Smad signaling are evolutionarily independent, our results suggest that IRF-3 originates from Smad and acquires its function downstream of TLR.

PubMed: 14555995
DOI: 10.1038/nsb1001

Experimental method

X-RAY DIFFRACTION (2.3 Å)