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5b32

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<StructureSection load='5b32' size='340' side='right'caption='[[5b32]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
<StructureSection load='5b32' size='340' side='right'caption='[[5b32]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5b32]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B32 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B32 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5b32]] 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=5B32 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B32 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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b33|5b33]], [[5b31|5b31]]</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=5b32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b32 OCA], [https://pdbe.org/5b32 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b32 RCSB], [https://www.ebi.ac.uk/pdbsum/5b32 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b32 ProSAT]</span></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=5b32 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b32 OCA], [http://pdbe.org/5b32 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b32 RCSB], [http://www.ebi.ac.uk/pdbsum/5b32 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b32 ProSAT]</span></td></tr>
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</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> [[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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[https://www.uniprot.org/uniprot/H33_HUMAN H33_HUMAN]
<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: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Arimura, Y]]
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[[Category: Arimura Y]]
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[[Category: Horikoshi, N]]
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[[Category: Horikoshi N]]
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[[Category: Kurumizaka, H]]
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[[Category: Kurumizaka H]]
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[[Category: Taguchi, H]]
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[[Category: Taguchi H]]
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[[Category: Dna binding protein]]
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[[Category: Histone variant]]
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[[Category: Nucleosome]]
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[[Category: Protein-dna complex]]
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Revision as of 06:37, 31 May 2023

The crystal structure of the heterotypic H2AZ/H2A nucleosome with H3.3.

PDB ID 5b32

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