BAUDIN, Antoine; GUICHARD, Anne; COLLIE, Gavin W.; ROUSSEAU, Sabrina; CHAIGNEPAIN, Stephane; HOCQUELLET, Agnes; BERBON, Melanie; LOQUET, Antoine; MACKERETH, Cameron; GUICHARD, Gilles; ODAERT, Benoit

doi:10.1007/s12104-018-9828-1

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BAUDIN, Antoine
Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

GUICHARD, Anne
Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

COLLIE, Gavin W.
Chimie et Biologie des Membranes et des Nanoobjets [CBMN]

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Biomolecular Nmr Assignments. 2018, vol. 12, n° 2, p. 309-314

Résumé en anglais

Death 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.< Réduire

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DR5

TRAIL

Cancer

Apoptosis

NMR spectroscopy

Resonance assignment

Secondary structure

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1H, 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)

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