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| | <StructureSection load='1u35' size='340' side='right'caption='[[1u35]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='1u35' size='340' side='right'caption='[[1u35]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1u35]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/ ], [http://en.wikipedia.org/wiki/Human Human] and [http://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 [http://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]] 3Å</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 ([http://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'>[http://proteopedia.org/fgij/fg.htm?mol=1u35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u35 OCA], [http://pdbe.org/1u35 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u35 RCSB], [http://www.ebi.ac.uk/pdbsum/1u35 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u35 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> [[http://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]]
| + | |
