5z30

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'''Unreleased structure'''
 
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The entry 5z30 is ON HOLD until Paper Publication
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==The crystal structure of the nucleosome containing a cancer-associated histone H2A.Z R80C mutant==
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<StructureSection load='5z30' size='340' side='right' caption='[[5z30]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
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Authors: Horikoshi, N., Arimura, Y., Kurumizaka, H.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5z30]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z30 FirstGlance]. <br>
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Description: The crystal structure of the nucleosome containing a cancer-associated histone H2A.Z R80C mutant
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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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[[Category: Unreleased Structures]]
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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=5z30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z30 OCA], [http://pdbe.org/5z30 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z30 RCSB], [http://www.ebi.ac.uk/pdbsum/5z30 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z30 ProSAT]</span></td></tr>
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</table>
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== 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> [[http://www.uniprot.org/uniprot/H2AZ_HUMAN H2AZ_HUMAN]] Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division.<ref>PMID:15878876</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Arimura, Y]]
[[Category: Arimura, Y]]
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[[Category: Horikoshi, N]]
[[Category: Kurumizaka, H]]
[[Category: Kurumizaka, H]]
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[[Category: Horikoshi, N]]
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[[Category: Chromatin]]
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[[Category: Chromatin formation]]
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[[Category: Dna binding]]
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[[Category: Dna binding protein-dna complex]]
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[[Category: Histone]]
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[[Category: Histone fold]]
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[[Category: Nucleosome]]
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[[Category: Nucleus]]

Revision as of 07:32, 18 July 2018

The crystal structure of the nucleosome containing a cancer-associated histone H2A.Z R80C mutant

5z30, resolution 2.45Å

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