1j2f
From Proteopedia
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'''X-ray crystal structure of IRF-3 and its functional implications''' | '''X-ray crystal structure of IRF-3 and its functional implications''' | ||
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[[Category: Takahasi, K.]] | [[Category: Takahasi, K.]] | ||
[[Category: Terasawa, H.]] | [[Category: Terasawa, H.]] | ||
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Revision as of 17:43, 2 May 2008
X-ray crystal structure of IRF-3 and its functional implications
Overview
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.
About this Structure
1J2F is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
X-ray crystal structure of IRF-3 and its functional implications., Takahasi K, Suzuki NN, Horiuchi M, Mori M, Suhara W, Okabe Y, Fukuhara Y, Terasawa H, Akira S, Fujita T, Inagaki F, Nat Struct Biol. 2003 Nov;10(11):922-7. Epub 2003 Oct 12. PMID:14555995 Page seeded by OCA on Fri May 2 20:43:22 2008
