1qwt: Difference between revisions

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[[Image:1qwt.~~jpg~~|left|200px]]

[[Image:1qwt.png|left|200px]]

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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.

The line below this paragraph, {{ABSTRACT_PUBMED_14555996}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 14555996 is the PubMed ID number.

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==About this Structure==

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[[Category: Qin, B Y.]]

[[Category: Dna binding protein]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 06~~:47:43 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:48:55 2008''

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-[[Image:1qwt.jpg|left|200px]]
+{{Seed}}
+[[Image:1qwt.png|left|200px]]
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 {{STRUCTURE_1qwt|  PDB=1qwt  |  SCENE=  }}
-'''Auto-inhibitory interferon regulation factor-3 (IRF3) transactivation domain'''
+===Auto-inhibitory interferon regulation factor-3 (IRF3) transactivation domain===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_14555996}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14555996 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14555996}}
 ==About this Structure==
@@ Line 24: / Line 28: @@
 [[Category: Qin, B Y.]]
 [[Category: Dna binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:47:43 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 04:48:55 2008''