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2o6g

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(New page: 200px<br /> <applet load="2o6g" size="450" color="white" frame="true" align="right" spinBox="true" caption="2o6g, resolution 3.100&Aring;" /> '''Crystal structure ...)
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[[Image:2o6g.gif|left|200px]]<br />
 
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<applet load="2o6g" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2o6g, resolution 3.100&Aring;" />
 
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'''Crystal structure of IRF-3 bound to the interferon-b enhancer'''<br />
 
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==Overview==
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==Crystal structure of IRF-3 bound to the interferon-b enhancer==
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Transcriptional activation of the interferon-beta (IFN-beta) gene requires, assembly of an enhanceosome containing ATF-2/c-Jun, IRF-3/IRF-7, and, NFkappaB. These factors bind cooperatively to the IFN-beta enhancer and, recruit coactivators and chromatin-remodeling proteins to the IFN-beta, promoter. We describe here a crystal structure of the DNA-binding domains, of IRF-3, IRF-7, and NFkappaB, bound to one half of the enhancer, and use, a previously described structure of the remaining half to assemble a, complete picture of enhanceosome architecture in the vicinity of the DNA., Association of eight proteins with the enhancer creates a continuous, surface for recognizing a composite DNA-binding element. Paucity of local, protein-protein contacts suggests that cooperative occupancy of the, enhancer comes from both binding-induced changes in DNA conformation and, interactions with additional components such as CBP. Contacts with, virtually every nucleotide pair account for the evolutionary invariance of, the enhancer sequence.
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<StructureSection load='2o6g' size='340' side='right'caption='[[2o6g]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2o6g]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The February 2010 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Enhanceosome'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2010_2 10.2210/rcsb_pdb/mom_2010_2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O6G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O6G FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o6g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o6g OCA], [https://pdbe.org/2o6g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o6g RCSB], [https://www.ebi.ac.uk/pdbsum/2o6g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o6g ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IRF3_HUMAN IRF3_HUMAN] Key transcriptional regulator of type I interferon (IFN)-dependent immune responses and plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, becomes phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o6/2o6g_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2o6g ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Transcriptional activation of the interferon-beta (IFN-beta) gene requires assembly of an enhanceosome containing ATF-2/c-Jun, IRF-3/IRF-7, and NFkappaB. These factors bind cooperatively to the IFN-beta enhancer and recruit coactivators and chromatin-remodeling proteins to the IFN-beta promoter. We describe here a crystal structure of the DNA-binding domains of IRF-3, IRF-7, and NFkappaB, bound to one half of the enhancer, and use a previously described structure of the remaining half to assemble a complete picture of enhanceosome architecture in the vicinity of the DNA. Association of eight proteins with the enhancer creates a continuous surface for recognizing a composite DNA-binding element. Paucity of local protein-protein contacts suggests that cooperative occupancy of the enhancer comes from both binding-induced changes in DNA conformation and interactions with additional components such as CBP. Contacts with virtually every nucleotide pair account for the evolutionary invariance of the enhancer sequence.
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==About this Structure==
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An atomic model of the interferon-beta enhanceosome.,Panne D, Maniatis T, Harrison SC Cell. 2007 Jun 15;129(6):1111-23. PMID:17574024<ref>PMID:17574024</ref>
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2O6G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2O6G OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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An Atomic Model of the Interferon-beta Enhanceosome., Panne D, Maniatis T, Harrison SC, Cell. 2007 Jun 15;129(6):1111-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17574024 17574024]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 2o6g" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Panne, D.]]
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[[Category: protein-dna complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:07:08 2007''
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==See Also==
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*[[Interferon regulatory factor|Interferon regulatory factor]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Enhanceosome]]
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: RCSB PDB Molecule of the Month]]
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[[Category: Panne D]]

Current revision

Crystal structure of IRF-3 bound to the interferon-b enhancer

PDB ID 2o6g

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