6vtx

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Current revision (08:20, 11 October 2023) (edit) (undo)
 
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==Crystal structure of human KLF4 zinc finger DNA binding domain in complex with NANOG DNA==
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<StructureSection load='6vtx' size='340' side='right'caption='[[6vtx]]' scene=''>
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<StructureSection load='6vtx' size='340' side='right'caption='[[6vtx]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6vtx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VTX FirstGlance]. <br>
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</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=6vtx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vtx OCA], [https://pdbe.org/6vtx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vtx RCSB], [https://www.ebi.ac.uk/pdbsum/6vtx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vtx ProSAT]</span></td></tr>
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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]] 2.14&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6vtx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vtx OCA], [https://pdbe.org/6vtx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vtx RCSB], [https://www.ebi.ac.uk/pdbsum/6vtx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vtx ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KLF4_HUMAN KLF4_HUMAN] Transcription factor; can act both as activator and as repressor. Binds the 5'-CACCC-3' core sequence. Binds to the promoter region of its own gene and can activate its own transcription. Regulates the expression of key transcription factors during embryonic development. Plays an important role in maintaining embryonic stem cells, and in preventing their differentiation. Required for establishing the barrier function of the skin and for postnatal maturation and maintenance of the ocular surface. Involved in the differentiation of epithelial cells and may also function in skeletal and kidney development. Contributes to the down-regulation of p53/TP53 transcription.<ref>PMID:17308127</ref> <ref>PMID:20071344</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Expression of a few master transcription factors can reprogram the epigenetic landscape and three-dimensional chromatin topology of differentiated cells and achieve pluripotency. During reprogramming, thousands of long-range chromatin contacts are altered, and changes in promoter association with enhancers dramatically influence transcription. Molecular participants at these sites have been identified, but how this re-organization might be orchestrated is not known. Biomolecular condensation is implicated in subcellular organization, including the recruitment of RNA polymerase in transcriptional activation. Here, we show that reprogramming factor KLF4 undergoes biomolecular condensation even in the absence of its intrinsically disordered region. Liquid-liquid condensation of the isolated KLF4 DNA binding domain with a DNA fragment from the NANOG proximal promoter is enhanced by CpG methylation of a KLF4 cognate binding site. We propose KLF4-mediated condensation as one mechanism for selectively organizing and re-organizing the genome based on the local sequence and epigenetic state.
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Liquid condensation of reprogramming factor KLF4 with DNA provides a mechanism for chromatin organization.,Sharma R, Choi KJ, Quan MD, Sharma S, Sankaran B, Park H, LaGrone A, Kim JJ, MacKenzie KR, Ferreon ACM, Kim C, Ferreon JC Nat Commun. 2021 Sep 22;12(1):5579. doi: 10.1038/s41467-021-25761-7. PMID:34552088<ref>PMID:34552088</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6vtx" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Z-disk]]
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[[Category: Choi KJ]]
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[[Category: Ferreon ACM]]
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[[Category: Ferreon JC]]
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[[Category: Kim C]]
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[[Category: MacKenzie KR]]
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[[Category: Sankaran B]]
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[[Category: Sharma R]]
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[[Category: Sharma S]]

Current revision

Crystal structure of human KLF4 zinc finger DNA binding domain in complex with NANOG DNA

PDB ID 6vtx

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