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6pa7
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The cryo-EM structure of the human DNMT3A2-DNMT3B3 complex bound to nucleosome.== |
| + | <StructureSection load='6pa7' size='340' side='right'caption='[[6pa7]], [[Resolution|resolution]] 2.94Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.94Å</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=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></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=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> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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. | ||
| - | + | ==See Also== | |
| - | + | *[[DNA methyltransferase 3D structures|DNA methyltransferase 3D structures]] | |
| - | + | *[[Histone 3D structures|Histone 3D structures]] | |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Xenopus laevis]] | ||
| + | [[Category: Jones PA]] | ||
| + | [[Category: Liang G]] | ||
| + | [[Category: Liu M]] | ||
| + | [[Category: Melcher K]] | ||
| + | [[Category: Xu HE]] | ||
| + | [[Category: Xu TH]] | ||
| + | [[Category: Zhao G]] | ||
| + | [[Category: Zhou XE]] | ||
Current revision
The cryo-EM structure of the human DNMT3A2-DNMT3B3 complex bound to nucleosome.
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Categories: Homo sapiens | Large Structures | Synthetic construct | Xenopus laevis | Jones PA | Liang G | Liu M | Melcher K | Xu HE | Xu TH | Zhao G | Zhou XE
