2rvq
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Solution structure of the isolated histone H2A-H2B heterodimer== | |
| + | <StructureSection load='2rvq' size='340' side='right' caption='[[2rvq]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2rvq]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RVQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RVQ FirstGlance]. <br> | ||
| + | </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=2rvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rvq OCA], [http://pdbe.org/2rvq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rvq RCSB], [http://www.ebi.ac.uk/pdbsum/2rvq PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | During chromatin-regulated processes, the histone H2A-H2B heterodimer functions dynamically in and out of the nucleosome. Although detailed crystal structures of nucleosomes have been established, that of the isolated full-length H2A-H2B heterodimer has remained elusive. Here, we have determined the solution structure of human H2A-H2B by NMR coupled with CS-Rosetta. H2A and H2B each contain a histone fold, comprising four alpha-helices and two beta-strands (alpha1-beta1-alpha2-beta2-alpha3-alphaC), together with the long disordered N- and C-terminal H2A tails and the long N-terminal H2B tail. The N-terminal alphaN helix, C-terminal beta3 strand, and 310 helix of H2A observed in the H2A-H2B nucleosome structure are disordered in isolated H2A-H2B. In addition, the H2A alpha1 and H2B alphaC helices are not well fixed in the heterodimer, and the H2A and H2B tails are not completely random coils. Comparison of hydrogen-deuterium exchange, fast hydrogen exchange, and {(1)H}-(15)N hetero-nuclear NOE data with the CS-Rosetta structure indicates that there is some conformation in the H2A 310 helical and H2B Lys11 regions, while the repression domain of H2B (residues 27-34) exhibits an extended string-like structure. This first structure of the isolated H2A-H2B heterodimer provides insight into its dynamic functions in chromatin. | ||
| - | + | Solution structure of the isolated histone H2A-H2B heterodimer.,Moriwaki Y, Yamane T, Ohtomo H, Ikeguchi M, Kurita J, Sato M, Nagadoi A, Shimojo H, Nishimura Y Sci Rep. 2016 May 16;6:24999. doi: 10.1038/srep24999. PMID:27181506<ref>PMID:27181506</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2rvq" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Ikeguchi, M]] | [[Category: Ikeguchi, M]] | ||
| - | [[Category: | + | [[Category: Kurita, J]] |
[[Category: Moriwaki, Y]] | [[Category: Moriwaki, Y]] | ||
| + | [[Category: Nagadoi, A]] | ||
| + | [[Category: Nishimura, Y]] | ||
[[Category: Ohtomo, H]] | [[Category: Ohtomo, H]] | ||
| - | [[Category: Kurita, J]] | ||
[[Category: Sato, M]] | [[Category: Sato, M]] | ||
| - | [[Category: Yamane, T]] | ||
[[Category: Shimojo, H]] | [[Category: Shimojo, H]] | ||
| + | [[Category: Yamane, T]] | ||
| + | [[Category: Cs-rosetta]] | ||
| + | [[Category: Dna binding protein]] | ||
| + | [[Category: H2a]] | ||
| + | [[Category: H2b]] | ||
| + | [[Category: Histone]] | ||
| + | [[Category: Nuclear protein-nuclear protein complex]] | ||
| + | [[Category: Nucleosome]] | ||
Revision as of 22:51, 1 June 2016
Solution structure of the isolated histone H2A-H2B heterodimer
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