1qwt: Difference between revisions

Revision as of 04:48, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1qwt.png

Template:STRUCTURE 1qwt

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

Template:ABSTRACT PUBMED 14555996

About this StructureAbout this Structure

1QWT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of IRF-3 reveals mechanism of autoinhibition and virus-induced phosphoactivation., Qin BY, Liu C, Lam SS, Srinath H, Delston R, Correia JJ, Derynck R, Lin K, Nat Struct Biol. 2003 Nov;10(11):913-21. Epub 2003 Oct 12. PMID:14555996

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Auto-inhibitory interferon regulation factor-3 (IRF3) transactivation domain'''
+===Auto-inhibitory interferon regulation factor-3 (IRF3) transactivation domain===
-==Overview==
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-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.
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