1u35: Difference between revisions

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<StructureSection load='1u35' size='340' side='right'caption='[[1u35]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='1u35' size='340' side='right'caption='[[1u35]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1u35]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/ ], [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U35 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1u35]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U35 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1aoi|1aoi]], [[1f66|1f66]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">H3FA, H3FC, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=1u35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u35 OCA], [https://pdbe.org/1u35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u35 RCSB], [https://www.ebi.ac.uk/pdbsum/1u35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u35 ProSAT]</span></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=1u35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u35 OCA], [https://pdbe.org/1u35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u35 RCSB], [https://www.ebi.ac.uk/pdbsum/1u35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u35 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>  [[https://www.uniprot.org/uniprot/H2B3A_MOUSE H2B3A_MOUSE]] Core component of nucleosome. 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.
[https://www.uniprot.org/uniprot/H31_MOUSE H31_MOUSE]  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Mus musculus]]
[[Category: Caron, C]]
[[Category: Caron C]]
[[Category: Chakravarthy, S]]
[[Category: Chakravarthy S]]
[[Category: Gundimella, S K]]
[[Category: Gundimella SK]]
[[Category: Khochbin, S]]
[[Category: Khochbin S]]
[[Category: Luger, K]]
[[Category: Luger K]]
[[Category: Pehrson, J R]]
[[Category: Pehrson JR]]
[[Category: Perche, P Y]]
[[Category: Perche PY]]
[[Category: Histone fold]]
[[Category: Histone variant]]
[[Category: Macroh2a]]
[[Category: Ncp]]
[[Category: Nucleosome]]
[[Category: Structural protein-dna complex]]

Latest revision as of 06:37, 23 August 2023

Crystal structure of the nucleosome core particle containing the histone domain of macroH2A

1u35, resolution 3.00Å

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