2l7e

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[[Image:2l7e.jpg|left|200px]]
 
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==The structure of a domain from yeast==
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The line below this paragraph, containing "STRUCTURE_2l7e", creates the "Structure Box" on the page.
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<StructureSection load='2l7e' size='340' side='right'caption='[[2l7e]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2l7e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L7E 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">Solution NMR</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=2l7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l7e OCA], [https://pdbe.org/2l7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l7e RCSB], [https://www.ebi.ac.uk/pdbsum/2l7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l7e ProSAT]</span></td></tr>
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{{STRUCTURE_2l7e| PDB=2l7e | SCENE= }}
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</table>
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== Function ==
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===The structure of a domain from yeast===
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[https://www.uniprot.org/uniprot/TAF14_YEAST TAF14_YEAST] Functions as a component of the DNA-binding general transcription factor complex TFIID, the RNA polymerase II associated general transcription factor complex TFIIF, and the chromatin-remodeling complex SWI/SNF. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. TFIIF is essential for the initiation of transcription by RNA polymerase II. TFIIF functions include the recruitment of RNA polymerase II to the promoter bound DNA-TBP-TFIIB complex, decreasing the affinity of RNA polymerase II for non-specific DNA, allowing for the subsequent recruitment of TFIIE and TFIIH, and facilitating RNA polymerase II elongation. The TAF14 subunit has stimulatory activity. Component of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. Component of the histone acetyltransferase NuA3 complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3. In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation.<ref>PMID:9618449</ref> <ref>PMID:10788514</ref> <ref>PMID:12138208</ref> <ref>PMID:12516863</ref> <ref>PMID:12672490</ref> <ref>PMID:17157260</ref>
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2l7e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L7E OCA].
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Tu, X.]]
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[[Category: Tu X]]
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[[Category: Zhang, J.]]
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[[Category: Zhang J]]
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[[Category: Zhang, W.]]
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[[Category: Zhang W]]

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The structure of a domain from yeast

PDB ID 2l7e

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