3w98: Difference between revisions
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==Crystal Structure of Human Nucleosome Core Particle lacking H3.1 N-terminal region== | |||
<StructureSection load='3w98' size='340' side='right'caption='[[3w98]], [[Resolution|resolution]] 3.42Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3w98]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W98 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.42Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=3w98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w98 OCA], [https://pdbe.org/3w98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w98 RCSB], [https://www.ebi.ac.uk/pdbsum/3w98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w98 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/H31_HUMAN H31_HUMAN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Histones are the protein components of the nucleosome, which forms the basic architecture of eukaryotic chromatin. Histones H2A, H2B, H3, and H4 are composed of two common regions, the "histone fold" and the "histone tail". Many efforts have been focused on the mechanisms by which the post-translational modifications of histone tails regulate the higher-order chromatin architecture. On the other hand, previous biochemical studies have suggested that histone tails also affect the structure and stability of the nucleosome core particle itself. However, the precise contributions of each histone tail are unclear. In the present study, we determined the crystal structures of four mutant nucleosomes, in which one of the four histones, H2A, H2B, H3, or H4, lacked the N-terminal tail. We found that the deletion of the H2B or H3 N-terminal tail affected histone-DNA interactions and substantially decreased nucleosome stability. These findings provide important information for understanding the complex roles of histone tails in regulating chromatin structure. | |||
Contribution of histone N-terminal tails to the structure and stability of nucleosomes.,Iwasaki W, Miya Y, Horikoshi N, Osakabe A, Taguchi H, Tachiwana H, Shibata T, Kagawa W, Kurumizaka H FEBS Open Bio. 2013 Aug 22;3:363-9. doi: 10.1016/j.fob.2013.08.007. PMID:24251097<ref>PMID:24251097</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3w98" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Histone 3D structures|Histone 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Horikoshi N]] | |||
[[Category: Iwasaki W]] | |||
[[Category: Kagawa W]] | |||
[[Category: Kurumizaka H]] | |||
[[Category: Miya Y]] | |||
[[Category: Osakabe A]] | |||
[[Category: Shibata T]] | |||
[[Category: Tachiwana H]] | |||
Latest revision as of 12:59, 8 November 2023
Crystal Structure of Human Nucleosome Core Particle lacking H3.1 N-terminal region
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