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PDBsum entry 6t7b
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Nuclear protein
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PDB id
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6t7b
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98 a.a.
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84 a.a.
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106 a.a.
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95 a.a.
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76 a.a.
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PDB id:
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| Name: |
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Nuclear protein
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Title:
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Structure of human sox2 transcription factor in complex with a nucleosome
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Structure:
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Histone h3.2. Chain: a, e. Synonym: histone h3/m,histone h3/o. Engineered: yes. Histone h4. Chain: b, f. Engineered: yes. Histone h2a type 1-b/e. Chain: c, g.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: hist2h3a, hist2h3c, h3f2, h3fm, hist2h3d. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: hist1h4a, h4/a, h4fa, hist1h4b, h4/i, h4fi, hist1h4c, h4/g, h4fg, hist1h4d, h4/b, h4fb, hist1h4e, h4/j, h4fj, hist1h4f, h4/c, h4fc, hist1h4h, h4/h, h4fh, hist1h4i, h4/m, h4fm, hist1h4j, h4/e,
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Authors:
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S.O.Dodonova,F.Zhu,C.Dienemann,J.Taipale,P.Cramer
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Key ref:
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S.O.Dodonova
et al.
(2020).
Nucleosome-bound SOX2 and SOX11 structures elucidate pioneer factor function.
Nature,
580,
669-672.
PubMed id:
DOI:
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Date:
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21-Oct-19
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Release date:
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29-Apr-20
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PROCHECK
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Headers
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References
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Q71DI3
(H32_HUMAN) -
Histone H3.2 from Homo sapiens
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Seq: Struc:
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136 a.a.
98 a.a.*
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P62805
(H4_HUMAN) -
Histone H4 from Homo sapiens
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Seq: Struc:
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103 a.a.
84 a.a.
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P04908
(H2A1B_HUMAN) -
Histone H2A type 1-B/E from Homo sapiens
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Seq: Struc:
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130 a.a.
106 a.a.
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Enzyme class:
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Chains A, B, C, D, E, F, G, H, K:
E.C.?
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DOI no:
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Nature
580:669-672
(2020)
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PubMed id:
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Nucleosome-bound SOX2 and SOX11 structures elucidate pioneer factor function.
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S.O.Dodonova,
F.Zhu,
C.Dienemann,
J.Taipale,
P.Cramer.
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ABSTRACT
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'Pioneer' transcription factors are required for stem-cell pluripotency, cell
differentiation and cell reprogramming1,2. 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 cells3. 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.
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');
}
}
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