2fxk: Difference between revisions
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==Crystal structure of the macro-domain of human core histone variant macroH2A1.1 (form A)== | ==Crystal structure of the macro-domain of human core histone variant macroH2A1.1 (form A)== | ||
<StructureSection load='2fxk' size='340' side='right' caption='[[2fxk]], [[Resolution|resolution]] 2.54Å' scene=''> | <StructureSection load='2fxk' size='340' side='right'caption='[[2fxk]], [[Resolution|resolution]] 2.54Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2fxk]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2fxk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1zq0 1zq0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FXK FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.54Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fxk OCA], [https://pdbe.org/2fxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fxk RCSB], [https://www.ebi.ac.uk/pdbsum/2fxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fxk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[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== | ||
*[[Histone|Histone]] | *[[Histone 3D structures|Histone 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Hothorn | [[Category: Large Structures]] | ||
[[Category: Kustatscher | [[Category: Hothorn M]] | ||
[[Category: Ladurner | [[Category: Kustatscher G]] | ||
[[Category: Pugieux | [[Category: Ladurner AG]] | ||
[[Category: Scheffzek | [[Category: Pugieux C]] | ||
[[Category: Scheffzek K]] | |||