6x0l
From Proteopedia
(Difference between revisions)
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- | ==== | + | ==Bridging of double-strand DNA break activates PARP2/HPF1 to modify chromatin== |
- | <StructureSection load='6x0l' size='340' side='right'caption='[[6x0l]]' scene=''> | + | <StructureSection load='6x0l' size='340' side='right'caption='[[6x0l]], [[Resolution|resolution]] 3.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6x0l]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6X0L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6X0L FirstGlance]. <br> |
- | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.9Å</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=6x0l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6x0l OCA], [https://pdbe.org/6x0l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6x0l RCSB], [https://www.ebi.ac.uk/pdbsum/6x0l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6x0l ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/HPF1_HUMAN HPF1_HUMAN] Acts as a cofactor for serine ADP-ribosylation by conferring serine specificity on PARP1 and PARP2: interacts with PARP1 and PARP2 and is able to change amino acid specificity toward serine (PubMed:28190768, PubMed:29480802). Promotes histone serine ADP-ribosylation in response to DNA damage, limiting DNA damage-induced PARP1 hyper-automodification, and ensuring genome stability (PubMed:27067600, PubMed:28190768). Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage (PubMed:29480802). HPF1 also promotes tyrosine ADP-ribosylation, probably by conferring tyrosine specificity on PARP1 (PubMed:30257210).<ref>PMID:27067600</ref> <ref>PMID:28190768</ref> <ref>PMID:29480802</ref> <ref>PMID:30257210</ref> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Poly(ADP-ribose) polymerase 3D structures|Poly(ADP-ribose) polymerase 3D structures]] | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Synthetic construct]] |
+ | [[Category: Bilokapic S]] | ||
+ | [[Category: Halic M]] |
Revision as of 14:47, 6 March 2024
Bridging of double-strand DNA break activates PARP2/HPF1 to modify chromatin
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