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| | <StructureSection load='6t78' size='340' side='right'caption='[[6t78]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='6t78' size='340' side='right'caption='[[6t78]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6t78]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T78 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6T78 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6t78]] is a 6 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=6T78 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T78 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SOX11 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.504Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6t78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t78 OCA], [http://pdbe.org/6t78 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t78 RCSB], [http://www.ebi.ac.uk/pdbsum/6t78 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t78 ProSAT]</span></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=6t78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t78 OCA], [https://pdbe.org/6t78 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t78 RCSB], [https://www.ebi.ac.uk/pdbsum/6t78 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t78 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/SOX11_HUMAN SOX11_HUMAN]] Coffin-Siris syndrome. The disease is caused by mutations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/SOX11_HUMAN SOX11_HUMAN] Coffin-Siris syndrome. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SOX11_HUMAN SOX11_HUMAN]] Transcription factor that acts as a transcriptional activator (PubMed:24886874). Binds cooperatively with POU3F2/BRN2 or POU3F1/OCT6 to gene promoters, which enhances transcriptional activation (By similarity). Acts as a transcriptional activator of TEAD2 by binding to its gene promoter and first intron (By similarity). Plays a redundant role with SOX4 and SOX12 in cell survival of developing tissues such as the neural tube, branchial arches and somites, thereby contributing to organogenesis (By similarity).[UniProtKB:Q7M6Y2]<ref>PMID:24886874</ref> | + | [https://www.uniprot.org/uniprot/SOX11_HUMAN SOX11_HUMAN] Transcription factor that acts as a transcriptional activator (PubMed:24886874). Binds cooperatively with POU3F2/BRN2 or POU3F1/OCT6 to gene promoters, which enhances transcriptional activation (By similarity). Acts as a transcriptional activator of TEAD2 by binding to its gene promoter and first intron (By similarity). Plays a redundant role with SOX4 and SOX12 in cell survival of developing tissues such as the neural tube, branchial arches and somites, thereby contributing to organogenesis (By similarity).[UniProtKB:Q7M6Y2]<ref>PMID:24886874</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cramer, P]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Dienemann, C]] | + | [[Category: Cramer P]] |
| - | [[Category: Dodonova, S O]] | + | [[Category: Dienemann C]] |
| - | [[Category: Taipale, J]] | + | [[Category: Dodonova SO]] |
| - | [[Category: Zhu, F]] | + | [[Category: Taipale J]] |
| - | [[Category: Dna]]
| + | [[Category: Zhu F]] |
| - | [[Category: Nuclear protein]]
| + | |
| - | [[Category: Pioneer factor]]
| + | |
| - | [[Category: Sox11]]
| + | |
| - | [[Category: Transcription factor]]
| + | |
| Structural highlights
Disease
SOX11_HUMAN Coffin-Siris syndrome. The disease is caused by mutations affecting the gene represented in this entry.
Function
SOX11_HUMAN Transcription factor that acts as a transcriptional activator (PubMed:24886874). Binds cooperatively with POU3F2/BRN2 or POU3F1/OCT6 to gene promoters, which enhances transcriptional activation (By similarity). Acts as a transcriptional activator of TEAD2 by binding to its gene promoter and first intron (By similarity). Plays a redundant role with SOX4 and SOX12 in cell survival of developing tissues such as the neural tube, branchial arches and somites, thereby contributing to organogenesis (By similarity).[UniProtKB:Q7M6Y2][1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tsurusaki Y, Koshimizu E, Ohashi H, Phadke S, Kou I, Shiina M, Suzuki T, Okamoto N, Imamura S, Yamashita M, Watanabe S, Yoshiura K, Kodera H, Miyatake S, Nakashima M, Saitsu H, Ogata K, Ikegawa S, Miyake N, Matsumoto N. De novo SOX11 mutations cause Coffin-Siris syndrome. Nat Commun. 2014 Jun 2;5:4011. doi: 10.1038/ncomms5011. PMID:24886874 doi:http://dx.doi.org/10.1038/ncomms5011
- ↑ Dodonova SO, Zhu F, Dienemann C, Taipale J, Cramer P. Nucleosome-bound SOX2 and SOX11 structures elucidate pioneer factor function. Nature. 2020 Apr;580(7805):669-672. doi: 10.1038/s41586-020-2195-y. Epub 2020 Apr, 22. PMID:32350470 doi:http://dx.doi.org/10.1038/s41586-020-2195-y
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