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5zbx

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m (Protected "5zbx" [edit=sysop:move=sysop])
Current revision (08:51, 22 November 2023) (edit) (undo)
 
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==The crystal structure of the nucleosome containing histone H3.1 CATD(V76Q, K77D)==
==The crystal structure of the nucleosome containing histone H3.1 CATD(V76Q, K77D)==
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<StructureSection load='5zbx' size='340' side='right' caption='[[5zbx]], [[Resolution|resolution]] 2.58&Aring;' scene=''>
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<StructureSection load='5zbx' size='340' side='right'caption='[[5zbx]], [[Resolution|resolution]] 2.58&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5zbx]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZBX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ZBX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5zbx]] is a 10 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=5ZBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZBX FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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]] 2.58&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5zbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zbx OCA], [http://pdbe.org/5zbx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5zbx RCSB], [http://www.ebi.ac.uk/pdbsum/5zbx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5zbx ProSAT]</span></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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=5zbx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zbx OCA], [https://pdbe.org/5zbx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zbx RCSB], [https://www.ebi.ac.uk/pdbsum/5zbx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zbx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/H2B1J_HUMAN H2B1J_HUMAN]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.<ref>PMID:11859126</ref> <ref>PMID:12860195</ref> <ref>PMID:15019208</ref> Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.<ref>PMID:11859126</ref> <ref>PMID:12860195</ref> <ref>PMID:15019208</ref>
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[https://www.uniprot.org/uniprot/H31_HUMAN H31_HUMAN] [https://www.uniprot.org/uniprot/CENPA_HUMAN CENPA_HUMAN] Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. The CENPA-H4 heterotetramer can bind DNA by itself (in vitro).<ref>PMID:20739937</ref> <ref>PMID:21478274</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>
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[[Category: Arimura, Y]]
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[[Category: Homo sapiens]]
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[[Category: Kurumizaka, H]]
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[[Category: Large Structures]]
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[[Category: Takagi, H]]
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[[Category: Arimura Y]]
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[[Category: Dna binding protein-dna complex]]
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[[Category: Kurumizaka H]]
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[[Category: Nucleosome]]
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[[Category: Takagi H]]

Current revision

The crystal structure of the nucleosome containing histone H3.1 CATD(V76Q, K77D)

PDB ID 5zbx

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