6t7d: Difference between revisions
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==Structure of human Sox11 transcription factor in complex with a nucleosome== | ==Structure of human Sox11 transcription factor in complex with a nucleosome== | ||
<StructureSection load='6t7d' size='340' side='right'caption='[[6t7d]]' scene=''> | <StructureSection load='6t7d' size='340' side='right'caption='[[6t7d]], [[Resolution|resolution]] 4.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T7D OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6t7d]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T7D FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.4Å</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=6t7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t7d OCA], [https://pdbe.org/6t7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t7d RCSB], [https://www.ebi.ac.uk/pdbsum/6t7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t7d ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/H32_HUMAN H32_HUMAN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
'Pioneer' transcription factors are required for stem-cell pluripotency, cell differentiation and cell reprogramming(1,2). Pioneer factors can bind nucleosomal DNA to enable gene expression from regions of the genome with closed chromatin. SOX2 is a prominent pioneer factor that is essential for pluripotency and self-renewal of embryonic stem cells(3). Here we report cryo-electron microscopy structures of the DNA-binding domains of SOX2 and its close homologue SOX11 bound to nucleosomes. The structures show that SOX factors can bind and locally distort DNA at superhelical location 2. The factors also facilitate detachment of terminal nucleosomal DNA from the histone octamer, which increases DNA accessibility. SOX-factor binding to the nucleosome can also lead to a repositioning of the N-terminal tail of histone H4 that includes residue lysine 16. We speculate that this repositioning is incompatible with higher-order nucleosome stacking, which involves contacts of the H4 tail with a neighbouring nucleosome. Our results indicate that pioneer transcription factors can use binding energy to initiate chromatin opening, and thereby facilitate nucleosome remodelling and subsequent transcription. | |||
Nucleosome-bound SOX2 and SOX11 structures elucidate pioneer factor function.,Dodonova SO, Zhu F, Dienemann C, Taipale J, Cramer P Nature. 2020 Apr;580(7805):669-672. doi: 10.1038/s41586-020-2195-y. Epub 2020 Apr, 22. PMID:32350470<ref>PMID:32350470</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6t7d" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Histone 3D structures|Histone 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Synthetic construct]] | |||
[[Category: Cramer P]] | [[Category: Cramer P]] | ||
[[Category: Dienemann C]] | [[Category: Dienemann C]] | ||
Latest revision as of 13:17, 22 May 2024
Structure of human Sox11 transcription factor in complex with a nucleosomeStructure of human Sox11 transcription factor in complex with a nucleosome
Structural highlights
FunctionPublication Abstract from PubMed'Pioneer' transcription factors are required for stem-cell pluripotency, cell differentiation and cell reprogramming(1,2). Pioneer factors can bind nucleosomal DNA to enable gene expression from regions of the genome with closed chromatin. SOX2 is a prominent pioneer factor that is essential for pluripotency and self-renewal of embryonic stem cells(3). Here we report cryo-electron microscopy structures of the DNA-binding domains of SOX2 and its close homologue SOX11 bound to nucleosomes. The structures show that SOX factors can bind and locally distort DNA at superhelical location 2. The factors also facilitate detachment of terminal nucleosomal DNA from the histone octamer, which increases DNA accessibility. SOX-factor binding to the nucleosome can also lead to a repositioning of the N-terminal tail of histone H4 that includes residue lysine 16. We speculate that this repositioning is incompatible with higher-order nucleosome stacking, which involves contacts of the H4 tail with a neighbouring nucleosome. Our results indicate that pioneer transcription factors can use binding energy to initiate chromatin opening, and thereby facilitate nucleosome remodelling and subsequent transcription. Nucleosome-bound SOX2 and SOX11 structures elucidate pioneer factor function.,Dodonova SO, Zhu F, Dienemann C, Taipale J, Cramer P Nature. 2020 Apr;580(7805):669-672. doi: 10.1038/s41586-020-2195-y. Epub 2020 Apr, 22. PMID:32350470[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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