2rvq: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2rvq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2RVQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[2rvq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/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'>[https://proteopedia.org/fgij/fg.htm?mol=2rvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rvq OCA], [https://pdbe.org/2rvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rvq RCSB], [https://www.ebi.ac.uk/pdbsum/2rvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rvq ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2rvq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rvq OCA], [https://pdbe.org/2rvq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rvq RCSB], [https://www.ebi.ac.uk/pdbsum/2rvq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rvq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/H2A1B_HUMAN H2A1B_HUMAN]  
[https://www.uniprot.org/uniprot/H2A1B_HUMAN H2A1B_HUMAN]  
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2rvq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
</StructureSection>

Latest revision as of 07:06, 1 May 2024

Solution structure of the isolated histone H2A-H2B heterodimer

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