5b33

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'''Unreleased structure'''
 
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The entry 5b33 is ON HOLD until Paper Publication
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==The crystal structure of the H2AZ nucleosome with H3.3.==
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<StructureSection load='5b33' size='340' side='right'caption='[[5b33]], [[Resolution|resolution]] 2.92&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5b33]] 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=5B33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B33 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.925&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5b33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b33 OCA], [https://pdbe.org/5b33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b33 RCSB], [https://www.ebi.ac.uk/pdbsum/5b33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b33 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/H33_HUMAN H33_HUMAN]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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H2A.Z is incorporated into nucleosomes located around transcription start sites and functions as an epigenetic regulator for the transcription of certain genes. During transcriptional regulation, the heterotypic H2A.Z/H2A nucleosome containing one each of H2A.Z and H2A is formed. However, previous homotypic H2A.Z nucleosome structures suggested that the L1 loop region of H2A.Z would sterically clash with the corresponding region of canonical H2A in the heterotypic nucleosome. To resolve this issue, we determined the crystal structures of heterotypic H2A.Z/H2A nucleosomes. In the H2A.Z/H2A nucleosome structure, the H2A.Z L1 loop structure was drastically altered without any structural changes of the canonical H2A L1 loop, thus avoiding the steric clash. Unexpectedly, the heterotypic H2A.Z/H2A nucleosome is more stable than the homotypic H2A.Z nucleosome. These data suggested that the flexible character of the H2A.Z L1 loop plays an essential role in forming the stable heterotypic H2A.Z/H2A nucleosome.
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Authors:
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Crystal structures of heterotypic nucleosomes containing histones H2A.Z and H2A.,Horikoshi N, Arimura Y, Taguchi H, Kurumizaka H Open Biol. 2016 Jun;6(6). pii: 160127. doi: 10.1098/rsob.160127. PMID:27358293<ref>PMID:27358293</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5b33" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Histone 3D structures|Histone 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Arimura Y]]
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[[Category: Horikoshi N]]
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[[Category: Kurumizaka H]]
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[[Category: Taguchi H]]

Current revision

The crystal structure of the H2AZ nucleosome with H3.3.

PDB ID 5b33

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