6ipu
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Human nucleosome core particle containing 145 bp of DNA== | |
| + | <StructureSection load='6ipu' size='340' side='right'caption='[[6ipu]], [[Resolution|resolution]] 1.99Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6ipu]] 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=6IPU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IPU FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.99Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=6ipu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ipu OCA], [https://pdbe.org/6ipu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ipu RCSB], [https://www.ebi.ac.uk/pdbsum/6ipu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ipu ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/H31_HUMAN H31_HUMAN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The poly(ADP-ribose) polymerase, PARP1, plays a key role in maintaining genomic integrity by detecting DNA damage and mediating repair. gammaH2A.X is the primary histone marker for DNA double-strand breaks and PARP1 localizes to H2A.X-enriched chromatin damage sites, but the basis for this association is not clear. We characterize the kinetics of PARP1 binding to a variety of nucleosomes harbouring DNA double-strand breaks, which reveal that PARP1 associates faster with (gamma)H2A.X- versus H2A-nucleosomes, resulting in a higher affinity for the former, which is maximal for gammaH2A.X-nucleosome that is also the activator eliciting the greatest poly-ADP-ribosylation catalytic efficiency. The enhanced activities with gammaH2A.X-nucleosome coincide with increased accessibility of the DNA termini resulting from the H2A.X-Ser139 phosphorylation. Indeed, H2A- and (gamma)H2A.X-nucleosomes have distinct stability characteristics, which are rationalized by mutational analysis and (gamma)H2A.X-nucleosome core crystal structures. This suggests that the gammaH2A.X epigenetic marker directly facilitates DNA repair by stabilizing PARP1 association and promoting catalysis. | ||
| - | + | PARP1 exhibits enhanced association and catalytic efficiency with gammaH2A.X-nucleosome.,Sharma D, De Falco L, Padavattan S, Rao C, Geifman-Shochat S, Liu CF, Davey CA Nat Commun. 2019 Dec 17;10(1):5751. doi: 10.1038/s41467-019-13641-0. PMID:31848352<ref>PMID:31848352</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Davey | + | <div class="pdbe-citations 6ipu" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | |
| + | ==See Also== | ||
| + | *[[Histone 3D structures|Histone 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Davey CA]] | ||
| + | [[Category: DeFalco L]] | ||
Current revision
Human nucleosome core particle containing 145 bp of DNA
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