1j2f: Difference between revisions

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==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.

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==

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[[Category: transcription factor]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 24: / Line 24: @@
 [[Category: transcription factor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:04:55 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:18:11 2008''