8v6v: Difference between revisions
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New page: '''Unreleased structure''' The entry 8v6v is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Cryo-EM structure of doubly-bound SNF2h-nucleosome complex== | |||
<StructureSection load='8v6v' size='340' side='right'caption='[[8v6v]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8v6v]] is a 12 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=8V6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8V6V 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]] 2.8Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=8v6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8v6v OCA], [https://pdbe.org/8v6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8v6v RCSB], [https://www.ebi.ac.uk/pdbsum/8v6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8v6v 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: Synthetic construct]] | |||
[[Category: Xenopus laevis]] | |||
[[Category: Armache JP]] | |||
[[Category: Cheng Y]] | |||
[[Category: Chio US]] | |||
[[Category: Narlikar GJ]] | |||
[[Category: Palovcak E]] | |||
Latest revision as of 11:22, 20 March 2024
Cryo-EM structure of doubly-bound SNF2h-nucleosome complexCryo-EM structure of doubly-bound SNF2h-nucleosome complex
Structural highlights
FunctionH32_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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