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3iid

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==Crystal structure of the macro domain of human histone macroH2A1.1 in complex with ADP-ribose (form A)==
==Crystal structure of the macro domain of human histone macroH2A1.1 in complex with ADP-ribose (form A)==
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<StructureSection load='3iid' size='340' side='right' caption='[[3iid]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='3iid' size='340' side='right'caption='[[3iid]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3iid]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IID OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IID FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3iid]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IID OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IID FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zr3|1zr3]], [[2fxk|2fxk]], [[3iif|3iif]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1zr3|1zr3]], [[2fxk|2fxk]], [[3iif|3iif]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">H2AFY, MACROH2A1, macroH2A1.1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">H2AFY, MACROH2A1, macroH2A1.1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3iid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iid OCA], [http://pdbe.org/3iid PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3iid RCSB], [http://www.ebi.ac.uk/pdbsum/3iid PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3iid ProSAT]</span></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=3iid FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iid OCA], [https://pdbe.org/3iid PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iid RCSB], [https://www.ebi.ac.uk/pdbsum/3iid PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iid ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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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[[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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
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*[[Histone|Histone]]
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*[[Histone 3D structures|Histone 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Bortfeld, M]]
[[Category: Bortfeld, M]]
[[Category: Hothorn, M]]
[[Category: Hothorn, M]]

Revision as of 03:33, 21 April 2022

Crystal structure of the macro domain of human histone macroH2A1.1 in complex with ADP-ribose (form A)

PDB ID 3iid

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