1zr3

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(New page: 200px<br /> <applet load="1zr3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zr3, resolution 1.66&Aring;" /> '''Crystal structure o...)
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[[Image:1zr3.gif|left|200px]]<br />
 
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<applet load="1zr3" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1zr3, resolution 1.66&Aring;" />
 
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'''Crystal structure of the macro-domain of human core histone variant macroH2A1.1 (form B)'''<br />
 
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==About this Structure==
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==Crystal structure of the macro-domain of human core histone variant macroH2A1.1 (form B)==
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1ZR3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MES as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZR3 OCA].
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<StructureSection load='1zr3' size='340' side='right'caption='[[1zr3]], [[Resolution|resolution]] 1.66&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1zr3]] is a 4 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=1ZR3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZR3 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]] 1.66&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></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=1zr3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zr3 OCA], [https://pdbe.org/1zr3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zr3 RCSB], [https://www.ebi.ac.uk/pdbsum/1zr3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zr3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/H2AY_HUMAN H2AY_HUMAN] Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. 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. Involved in stable X chromosome inactivation. Inhibits the binding of transcription factors and interferes with the activity of remodeling SWI/SNF complexes. Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin. In addition, isoform 1, but not isoform 2, binds ADP-ribose and O-acetyl-ADP-ribose, and may be involved in ADP-ribose-mediated chromatin modulation.<ref>PMID:12718888</ref> <ref>PMID:15621527</ref> <ref>PMID:15897469</ref> <ref>PMID:16428466</ref> <ref>PMID:16107708</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zr/1zr3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zr3 ConSurf].
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<div style="clear:both"></div>
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==Reference==
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==See Also==
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Getting a grip on O-acetyl-ADP-ribose., Hoff KG, Wolberger C, Nat Struct Mol Biol. 2005 Jul;12(7):560-1. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15999106 15999106]
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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>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hothorn, M.]]
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[[Category: Hothorn M]]
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[[Category: Kustatscher, G.]]
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[[Category: Kustatscher G]]
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[[Category: Ladurner, A.G.]]
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[[Category: Ladurner AG]]
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[[Category: Pugieux, C.]]
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[[Category: Pugieux C]]
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[[Category: Scheffzek, K.]]
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[[Category: Scheffzek K]]
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[[Category: MES]]
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[[Category: a1pp]]
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[[Category: chromatin]]
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[[Category: histone]]
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[[Category: macro-domain]]
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[[Category: p-loop]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:39:34 2007''
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Current revision

Crystal structure of the macro-domain of human core histone variant macroH2A1.1 (form B)

PDB ID 1zr3

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