8ruq
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Borealin N-terminus in complex with H3.T3p-nucleosome== | |
| - | + | <StructureSection load='8ruq' size='340' side='right'caption='[[8ruq]], [[Resolution|resolution]] 2.29Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8ruq]] is a 11 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/Unidentified Unidentified]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8RUQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8RUQ 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]] 2.29Å</td></tr> | |
| - | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</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=8ruq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ruq OCA], [https://pdbe.org/8ruq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ruq RCSB], [https://www.ebi.ac.uk/pdbsum/8ruq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ruq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/H32_XENLA H32_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. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Unidentified]] | ||
| + | [[Category: Xenopus laevis]] | ||
| + | [[Category: Barr FA]] | ||
| + | [[Category: Ruza RR]] | ||
Current revision
Borealin N-terminus in complex with H3.T3p-nucleosome
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