6pa7

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'''Unreleased structure'''
 
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The entry 6pa7 is ON HOLD until Paper Publication
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==The cryo-EM structure of the human DNMT3A2-DNMT3B3 complex bound to nucleosome.==
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<StructureSection load='6pa7' size='340' side='right'caption='[[6pa7]], [[Resolution|resolution]] 2.94&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6pa7]] is a 14 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PA7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PA7 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.94&#8491;</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=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=6pa7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pa7 OCA], [https://pdbe.org/6pa7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pa7 RCSB], [https://www.ebi.ac.uk/pdbsum/6pa7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pa7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/H4_XENLA H4_XENLA] 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.
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Authors:
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==See Also==
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*[[DNA methyltransferase 3D structures|DNA methyltransferase 3D structures]]
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Description:
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*[[Histone 3D structures|Histone 3D structures]]
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[[Category: Unreleased Structures]]
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Synthetic construct]]
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[[Category: Xenopus laevis]]
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[[Category: Jones PA]]
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[[Category: Liang G]]
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[[Category: Liu M]]
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[[Category: Melcher K]]
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[[Category: Xu HE]]
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[[Category: Xu TH]]
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[[Category: Zhao G]]
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[[Category: Zhou XE]]

Current revision

The cryo-EM structure of the human DNMT3A2-DNMT3B3 complex bound to nucleosome.

PDB ID 6pa7

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