1qwt: Difference between revisions
New page: left|200px<br /> <applet load="1qwt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qwt, resolution 2.1Å" /> '''Auto-inhibitory inte... |
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'''Auto-inhibitory interferon regulation factor-3 (IRF3) transactivation domain'''<br /> | '''Auto-inhibitory interferon regulation factor-3 (IRF3) transactivation domain'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1QWT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1QWT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWT OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: dna binding protein]] | [[Category: dna binding protein]] | ||
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Revision as of 17:46, 15 February 2008
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Auto-inhibitory interferon regulation factor-3 (IRF3) transactivation domain
OverviewOverview
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.
About this StructureAbout this Structure
1QWT is a Single protein structure of sequence from Homo sapiens with as ligand. 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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