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dc.contributor.authorZaleska, Men_US
dc.contributor.authorPollock, Ken_US
dc.contributor.authorCollins, Ien_US
dc.contributor.authorGuettler, Sen_US
dc.contributor.authorPfuhl, Men_US
dc.coverage.spatialNetherlandsen_US
dc.date.accessioned2019-03-11T12:05:39Z
dc.date.issued2019-04en_US
dc.identifierhttps://www.ncbi.nlm.nih.gov/pubmed/30847846en_US
dc.identifier10.1007/s12104-019-09887-wen_US
dc.identifier.citationBiomol NMR Assign, 2019, 13 (1), pp. 255 - 260en_US
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/3147
dc.identifier.eissn1874-270Xen_US
dc.identifier.doi10.1007/s12104-019-09887-wen_US
dc.description.abstractTankyrases are poly(ADP-ribose)polymerases (PARPs) which recognize their substrates via their ankyrin repeat cluster (ARC) domains. The human tankyrases (TNKS/TNKS2) contain five ARCs in their extensive N-terminal region; of these, four bind peptides present within tankyrase interactors and substrates. These short, linear segments, known as tankyrase-binding motifs (TBMs), contain some highly conserved features: an arginine at position 1, which occupies a predominantly acidic binding site, and a glycine at position 6 that is sandwiched between two aromatic side chains on the surface of the ARC domain. Tankyrases are involved in a multitude of biological functions, amongst them Wnt/β-catenin signaling, the maintenance of telomeres, glucose metabolism, spindle formation, the DNA damage response and Hippo signaling. As many of these are relevant to human disease, tankyrase is an important target candidate for drug development. With the emergence of non-catalytic (scaffolding) functions of tankyrase, it seems attractive to interfere with ARC function rather than the enzymatic activity of tankyrase. To study the mechanism of ARC-dependent recruitment of tankyrase binders and enable protein-observed NMR screening methods, we have as the first step obtained a full backbone and partial side chain assignment of TNKS2 ARC4. The assignment highlights some of the unusual structural features of the ARC domain.en_US
dc.format.extent255 - 260en_US
dc.languageengen_US
dc.language.isoengen_US
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en_US
dc.subjectADP-ribosylationen_US
dc.subjectAnkyrin repeatsen_US
dc.subjectSignalingen_US
dc.subjectUbiquitylationen_US
dc.titleSolution NMR assignment of the ARC4 domain of human tankyrase 2.en_US
dc.typeJournal Article
dcterms.dateAccepted2019-03-02en_US
rioxxterms.versionofrecord10.1007/s12104-019-09887-wen_US
rioxxterms.licenseref.startdate2019-04en_US
rioxxterms.typeJournal Article/Reviewen_US
dc.relation.isPartOfBiomol NMR Assignen_US
pubs.issue1en_US
pubs.notesNo embargoen_US
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Cancer Therapeutics
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Cancer Therapeutics/Medicinal Chemistry 2
pubs.publication-statusPublisheden_US
pubs.volume13en_US
pubs.embargo.termsNo embargoen_US
icr.researchteamMedicinal Chemistry 2en_US
dc.contributor.icrauthorCollins, Ianen_US


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