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- Title
X-ray crystal structure of IRF-3 and its functional implications.
- Authors
Takahasi, Kiyohiro; Suzuki, Nobuo N; Horiuchi, Masataka; Mori, Mitsuaki; Suhara, Wakako; Okabe, Yasutaka; Fukuhara, Yukiko; Terasawa, Hiroaki; Akira, Shizuo; Fujita, Takashi; Inagaki, Fuyuhiko
- 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.
- Publication
Nature structural biology, 2003, Vol 10, Issue 11, p922
- ISSN
1072-8368
- Publication type
Journal Article
- DOI
10.1038/nsb1001