View source for 2li6


==1H, 13C, and 15N Chemical Shift Assignments for yeast protein==
<StructureSection load='2li6' size='340' side='right'caption='[[2li6]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2li6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LI6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2li6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2li6 OCA], [https://pdbe.org/2li6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2li6 RCSB], [https://www.ebi.ac.uk/pdbsum/2li6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2li6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SWI1_YEAST SWI1_YEAST] Involved in transcriptional activation. Component of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, which 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.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
SWI1 is a subunit of the SWI/SNF complex involved in chromatin remodeling. It contains an AT-rich interaction domain (ARID) which has the potential DNA binding activity. In this study, we determined the solution structure of the SWI1 ARID domain from Saccharomyces cerevisiae by NMR spectroscopy. Yeast SWI1 ARID domain is composed of seven alpha-helices,6 of which are conserved among the ARID family. In addition, the DNA binding activity of the SWI1 ARID domain was confirmed by chemical shift perturbation assay. Similar to its human homologous, the yeast SWI1 ARID domain binds DNA non-specifically. Proteins 2012. (c) 2012 Wiley-Liss, Inc.

Solution structure of SWI1 ARID domain from Saccharomyces cerevisiae and its non-specific binding to DNA.,Wang T, Zhang J, Zhang X, Tu X Proteins. 2012 Apr 10. doi: 10.1002/prot.24091. PMID:22488857<ref>PMID:22488857</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2li6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Tu X]]
[[Category: Wang T]]
[[Category: Zhang J]]