3av1
From Proteopedia
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| - | [[Image:3av1.png|left|200px]] | ||
| - | < | + | ==The human nucleosome structure containing the histone variant H3.2== |
| - | + | <StructureSection load='3av1' size='340' side='right'caption='[[3av1]], [[Resolution|resolution]] 2.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3av1]] 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=3AV1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AV1 FirstGlance]. <br> | |
| - | or | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=3av1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3av1 OCA], [https://pdbe.org/3av1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3av1 RCSB], [https://www.ebi.ac.uk/pdbsum/3av1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3av1 ProSAT]</span></td></tr> |
| - | + | </table> | |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/H32_HUMAN H32_HUMAN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The nucleosome is the fundamental repeating unit of chromatin, via which genomic DNA is packaged into the nucleus in eukaryotes. In the nucleosome, two copies of each core histone, H2A, H2B, H3 and H4, form a histone octamer which wraps 146 base pairs of DNA around itself. All of the core histones except for histone H4 have nonallelic isoforms called histone variants. In humans, eight histone H3 variants, H3.1, H3.2, H3.3, H3T, H3.5, H3.X, H3.Y and CENP-A, have been reported to date. Previous studies have suggested that histone H3 variants possess distinct functions in the formation of specific chromosome regions and/or in the regulation of transcription and replication. H3.1, H3.2 and H3.3 are the most abundant H3 variants. Here, crystal structures of human nucleosomes containing either H3.2 or H3.3 have been solved. The structures were essentially the same as that of the H3.1 nucleosome. Since the amino-acid residues specific for H3.2 and H3.3 are located on the accessible surface of the H3/H4 tetramer, they may be potential interaction sites for H3.2- and H3.3-specific chaperones. | ||
| - | + | Structures of human nucleosomes containing major histone H3 variants.,Tachiwana H, Osakabe A, Shiga T, Miya Y, Kimura H, Kagawa W, Kurumizaka H Acta Crystallogr D Biol Crystallogr. 2011 Jun;67(Pt 6):578-83. Epub 2011 May 17. PMID:21636898<ref>PMID:21636898</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3av1" style="background-color:#fffaf0;"></div> | |
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| - | == | + | |
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==See Also== | ==See Also== | ||
| - | *[[Histone|Histone]] | + | *[[Histone 3D structures|Histone 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Kagawa | + | [[Category: Large Structures]] |
| - | [[Category: Kimura | + | [[Category: Kagawa W]] |
| - | [[Category: Kurumizaka | + | [[Category: Kimura H]] |
| - | [[Category: Miya | + | [[Category: Kurumizaka H]] |
| - | [[Category: Osakabe | + | [[Category: Miya Y]] |
| - | [[Category: Shiga | + | [[Category: Osakabe A]] |
| - | [[Category: Tachiwana | + | [[Category: Shiga T]] |
| - | + | [[Category: Tachiwana H]] | |
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Current revision
The human nucleosome structure containing the histone variant H3.2
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Categories: Homo sapiens | Large Structures | Kagawa W | Kimura H | Kurumizaka H | Miya Y | Osakabe A | Shiga T | Tachiwana H
