5lw6

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m (Protected "5lw6" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5lw6 is ON HOLD
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==Crystal structure of a Se-Met substituted Dictyostelium discoideum ADP-ribose binding macrodomain (residues 342-563) of DDB_G0293866==
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<StructureSection load='5lw6' size='340' side='right' caption='[[5lw6]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5lw6]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LW6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LW6 FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<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=5lw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lw6 OCA], [http://pdbe.org/5lw6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lw6 RCSB], [http://www.ebi.ac.uk/pdbsum/5lw6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lw6 ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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ADP-ribosylation by ADP-ribosyltransferases (ARTs) has a well-established role in DNA strand break repair by promoting enrichment of repair factors at damage sites through ADP-ribose interaction domains. Here we exploit the simple eukaryote Dictyostelium to uncover a role for ADP-ribosylation in regulating DNA interstrand crosslink repair and redundancy of this pathway with non-homologous end-joining (NHEJ). In silico searches identify a protein that contains a permutated macrodomain (Aprataxin/APLF-and-PNKP-Like protein; APL). Structural analysis reveals permutated macrodomains retain features associated with ADP-ribose interactions and APL is capable of binding poly-ADP-ribose through its macrodomain. APL is enriched in chromatin in response to cisplatin, an agent that induces DNA interstrand crosslinks (ICLs). This is dependent on the macrodomain of APL, and the ART Adprt2, indicating a role for ADP-ribosylation in the cellular response to cisplatin. Although adprt2- cells are sensitive to cisplatin, ADP-ribosylation is evident in these cells due to redundant signalling by the DSB-responsive ART Adprt1a, promoting NHEJ-mediated repair. These data implicate ADP-ribosylation in DNA ICL repair and identify NHEJ can function to resolve this form of DNA damage in the absence of Adprt2.
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Authors: Leys, D., Barkauskaite, E., Pinero, B.B., Ahel, I.
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The role of ADP-ribosylation in regulating DNA interstrand crosslink repair.,Gunn AR, Banos-Pinero B, Paschke P, Sanchez-Pulido L, Ariza A, Day J, Emrich M, Leys D, Ponting CP, Ahel I, Lakin ND J Cell Sci. 2016 Sep 1. pii: jcs.193375. PMID:27587838<ref>PMID:27587838</ref>
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Description: Crystal structure of a Se-Met substituted Dictyostelium discoideum ADP-ribose binding macrodomain (residues 342-563) of DDB_G0293866
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Leys, D]]
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<div class="pdbe-citations 5lw6" style="background-color:#fffaf0;"></div>
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[[Category: Barkauskaite, E]]
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== References ==
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[[Category: Pinero, B.B]]
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<references/>
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__TOC__
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</StructureSection>
[[Category: Ahel, I]]
[[Category: Ahel, I]]
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[[Category: Barkauskaite, E]]
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[[Category: Leys, D]]
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[[Category: Pinero, B B]]
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[[Category: Adp-ribose binding protein]]
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[[Category: Macrodomain]]

Revision as of 16:52, 3 October 2016

Crystal structure of a Se-Met substituted Dictyostelium discoideum ADP-ribose binding macrodomain (residues 342-563) of DDB_G0293866

5lw6, resolution 1.80Å

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