5fug

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'''Unreleased structure'''
 
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The entry 5fug is ON HOLD until Paper Publication
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==Crystal structure of a human YL1-H2A.Z-H2B complex==
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<StructureSection load='5fug' size='340' side='right' caption='[[5fug]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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Authors: Marek, M., Romier, C.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5fug]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FUG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FUG FirstGlance]. <br>
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Description: Crystal structure of a human YL1-H2A.Z-H2B complex
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fue|5fue]]</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=5fug FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fug OCA], [http://pdbe.org/5fug PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fug RCSB], [http://www.ebi.ac.uk/pdbsum/5fug PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[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> [[http://www.uniprot.org/uniprot/VPS72_HUMAN VPS72_HUMAN]] Could be a DNA-binding transcriptional regulator. May be involved in chromatin modification and remodeling. [[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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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Dimitrov, S]]
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[[Category: Ennifar, E]]
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[[Category: Hamiche, A]]
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[[Category: Ignatyeva, M]]
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[[Category: Latrick, C M]]
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[[Category: Marek, M]]
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[[Category: Obri, A]]
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[[Category: Ouararhni, K]]
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[[Category: Papin, C]]
[[Category: Romier, C]]
[[Category: Romier, C]]
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[[Category: Marek, M]]
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[[Category: Stoll, I]]
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[[Category: Chaperone]]
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[[Category: Dna binding protein]]
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[[Category: H2a z]]
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[[Category: Histone]]
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[[Category: Remodeler]]
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[[Category: Yl1]]

Revision as of 03:57, 10 March 2016

Crystal structure of a human YL1-H2A.Z-H2B complex

5fug, resolution 2.70Å

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