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5chl

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==Structural basis of H2A.Z recognition by YL1 histone chaperone component of SRCAP/SWR1 chromatin remodeling complex==
==Structural basis of H2A.Z recognition by YL1 histone chaperone component of SRCAP/SWR1 chromatin remodeling complex==
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<StructureSection load='5chl' size='340' side='right' caption='[[5chl]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
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<StructureSection load='5chl' size='340' side='right'caption='[[5chl]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5chl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CHL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CHL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5chl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CHL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CHL FirstGlance]. <br>
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</td></tr><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=5chl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5chl OCA], [http://pdbe.org/5chl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5chl RCSB], [http://www.ebi.ac.uk/pdbsum/5chl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5chl ProSAT]</span></td></tr>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5chl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5chl OCA], [https://pdbe.org/5chl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5chl RCSB], [https://www.ebi.ac.uk/pdbsum/5chl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5chl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/VPS72_DROME VPS72_DROME]] Part of the Tip60 chromatin-remodeling complex which is involved in DNA repair. Upon induction of DNA double-strand breaks, this complex acetylates phosphorylated H2AV in nucleosomes and exchanges it with unmodified H2AV.<ref>PMID:15528408</ref> <ref>PMID:16299513</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/VPS72_DROME VPS72_DROME] Part of the Tip60 chromatin-remodeling complex which is involved in DNA repair. Upon induction of DNA double-strand breaks, this complex acetylates phosphorylated H2AV in nucleosomes and exchanges it with unmodified H2AV.<ref>PMID:15528408</ref> <ref>PMID:16299513</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5chl" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5chl" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Liang, X]]
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[[Category: Drosophila melanogaster]]
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[[Category: Pan, L]]
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[[Category: Homo sapiens]]
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[[Category: Shan, S]]
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[[Category: Large Structures]]
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[[Category: Wu, C]]
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[[Category: Liang X]]
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[[Category: Zhou, Z]]
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[[Category: Pan L]]
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[[Category: Chaperone]]
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[[Category: Shan S]]
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[[Category: Histone]]
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[[Category: Wu C]]
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[[Category: Remodeling complex]]
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[[Category: Zhou Z]]

Current revision

Structural basis of H2A.Z recognition by YL1 histone chaperone component of SRCAP/SWR1 chromatin remodeling complex

PDB ID 5chl

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