1qwt: Difference between revisions
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'''Auto-inhibitory interferon regulation factor-3 (IRF3) transactivation domain''' | {{Structure | ||
|PDB= 1qwt |SIZE=350|CAPTION= <scene name='initialview01'>1qwt</scene>, resolution 2.1Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | |||
|ACTIVITY= | |||
|GENE= IRF3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Auto-inhibitory interferon regulation factor-3 (IRF3) transactivation domain''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1QWT is a [ | 1QWT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWT OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14555996 14555996] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: dna binding protein]] | [[Category: dna binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:43:47 2008'' | ||
Revision as of 14:43, 20 March 2008
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| , resolution 2.1Å | |||||||
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| Ligands: | |||||||
| Gene: | IRF3 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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