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| | <StructureSection load='5b33' size='340' side='right'caption='[[5b33]], [[Resolution|resolution]] 2.92Å' scene=''> | | <StructureSection load='5b33' size='340' side='right'caption='[[5b33]], [[Resolution|resolution]] 2.92Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5b33]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B33 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B33 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5b33]] is a 10 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=5B33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5B33 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b32|5b32]], [[5b31|5b31]]</td></tr> | + | </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=5b33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b33 OCA], [https://pdbe.org/5b33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5b33 RCSB], [https://www.ebi.ac.uk/pdbsum/5b33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5b33 ProSAT]</span></td></tr> |
| - | <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=5b33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b33 OCA], [http://pdbe.org/5b33 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b33 RCSB], [http://www.ebi.ac.uk/pdbsum/5b33 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b33 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/H2B1J_HUMAN H2B1J_HUMAN]] 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.<ref>PMID:11859126</ref> <ref>PMID:12860195</ref> <ref>PMID:15019208</ref> Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.<ref>PMID:11859126</ref> <ref>PMID:12860195</ref> <ref>PMID:15019208</ref> [[http://www.uniprot.org/uniprot/H2AZ_HUMAN H2AZ_HUMAN]] Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division.<ref>PMID:15878876</ref> | + | [https://www.uniprot.org/uniprot/H33_HUMAN H33_HUMAN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Arimura, Y]] | + | [[Category: Arimura Y]] |
| - | [[Category: Horikoshi, N]] | + | [[Category: Horikoshi N]] |
| - | [[Category: Kurumizaka, H]] | + | [[Category: Kurumizaka H]] |
| - | [[Category: Taguchi, H]] | + | [[Category: Taguchi H]] |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Histone variant]]
| + | |
| - | [[Category: Nucleosome]]
| + | |
| - | [[Category: Protein-dna complex]]
| + | |
| Structural highlights
Function
H33_HUMAN
Publication Abstract from PubMed
H2A.Z is incorporated into nucleosomes located around transcription start sites and functions as an epigenetic regulator for the transcription of certain genes. During transcriptional regulation, the heterotypic H2A.Z/H2A nucleosome containing one each of H2A.Z and H2A is formed. However, previous homotypic H2A.Z nucleosome structures suggested that the L1 loop region of H2A.Z would sterically clash with the corresponding region of canonical H2A in the heterotypic nucleosome. To resolve this issue, we determined the crystal structures of heterotypic H2A.Z/H2A nucleosomes. In the H2A.Z/H2A nucleosome structure, the H2A.Z L1 loop structure was drastically altered without any structural changes of the canonical H2A L1 loop, thus avoiding the steric clash. Unexpectedly, the heterotypic H2A.Z/H2A nucleosome is more stable than the homotypic H2A.Z nucleosome. These data suggested that the flexible character of the H2A.Z L1 loop plays an essential role in forming the stable heterotypic H2A.Z/H2A nucleosome.
Crystal structures of heterotypic nucleosomes containing histones H2A.Z and H2A.,Horikoshi N, Arimura Y, Taguchi H, Kurumizaka H Open Biol. 2016 Jun;6(6). pii: 160127. doi: 10.1098/rsob.160127. PMID:27358293[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Horikoshi N, Arimura Y, Taguchi H, Kurumizaka H. Crystal structures of heterotypic nucleosomes containing histones H2A.Z and H2A. Open Biol. 2016 Jun;6(6). pii: 160127. doi: 10.1098/rsob.160127. PMID:27358293 doi:http://dx.doi.org/10.1098/rsob.160127
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