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dc.rights.licenseopenen_US
dc.relation.isnodoubleb5324c18-82cf-442e-acda-e23e977e57de*
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorBAUDIN, Antoine
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorGUICHARD, Anne
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorCOLLIE, Gavin W.
hal.structure.identifierARNA - Acides Nucléiques : Régulations Naturelle et Artificielle
dc.contributor.authorROUSSEAU, Sabrina
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorCHAIGNEPAIN, Stephane
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHOCQUELLET, Agnes
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorBERBON, Melanie
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLOQUET, Antoine
hal.structure.identifierARNA - Acides Nucléiques : Régulations Naturelle et Artificielle
dc.contributor.authorMACKERETH, Cameron
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorGUICHARD, Gilles
IDREF: 084339268
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorODAERT, Benoit
dc.date.accessioned2020-04-17T10:11:21Z
dc.date.available2020-04-17T10:11:21Z
dc.date.issued2018
dc.identifier.issn1874-2718en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/4295
dc.description.abstractEnDeath receptors (DR) selectively drive cancer cells to apoptosis upon binding to the Tumor necrosis factor-a-Related Apoptosis-Inducing Ligand (TRAIL). Complex formation induces the oligomerization of the death receptors DR4 (TRAIL-R1) and DR5 (TRAIL-R2) and transduces the apoptogenic signal to their respective death domains, leading to Death Inducing Signaling Complex (DISC) formation, caspase activation and ultimately cell death. Several crystal structures of the ExtraCellular Domain from Death Receptor 5 (DR5-ECD) have been reported in complex with the TRAIL ligand or anti-DR5 antibodies, but none for the isolated protein. In order to fill this gap and to perform binding experiments with TRAIL peptidomimetics, we have produced isotopically labelled DR5-ECD and started a conformational analysis by using high-field 3D NMR spectroscopy. Herein, we present the first resonance assignment of a TRAIL receptor in solution and the determination of its secondary structure from NMR chemical shifts.
dc.language.isoENen_US
dc.subject.enDR5
dc.subject.enTRAIL
dc.subject.enCancer
dc.subject.enApoptosis
dc.subject.enNMR spectroscopy
dc.subject.enResonance assignment
dc.subject.enSecondary structure
dc.title.en1H, 13C, 15N NMR resonance assignments and secondary structure determination of the extra-cellular domain from the human proapoptotic TRAIL-R2 death receptor 5 (DR5-ECD)
dc.title.alternativeBiomol NMR Assignen_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1007/s12104-018-9828-1
dc.subject.halChimie/Matériauxen_US
bordeaux.journalBiomolecular Nmr Assignmentsen_US
bordeaux.page309-314en_US
bordeaux.volume12en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248
bordeaux.issue2en_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.identifier.funderIDLigue Contre le Canceren_US
hal.identifierhal-03184395
hal.version1
hal.date.transferred2021-03-29T12:21:27Z
hal.exporttrue
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