TNFRSF10B

1D0G, 1D4V, 1DU3, 1ZA3, 2H9G, 4I9X, 4N90, 4OD2, 3X3F8795n/aENSG00000120889n/aO14763n/aNM_003842NM_147187n/aNP_003833NP_671716n/aDeath receptor 5 (DR5), also known as TRAIL receptor 2 (TRAILR2) and tumor necrosis factor receptor superfamily member 10B (TNFRSF10B), is a cell surface receptor of the TNF-receptor superfamily that binds TRAIL and mediates apoptosis.1d0g: CRYSTAL STRUCTURE OF DEATH RECEPTOR 5 (DR5) BOUND TO APO2L/TRAIL1d4v: Crystal structure of trail-DR5 complex1du3: Crystal structure of TRAIL-SDR51za3: The crystal structure of the YSd1 Fab bound to DR52h9g: Crystal structure of phage derived Fab BdF1 with human Death Receptor 5 (DR5) Death receptor 5 (DR5), also known as TRAIL receptor 2 (TRAILR2) and tumor necrosis factor receptor superfamily member 10B (TNFRSF10B), is a cell surface receptor of the TNF-receptor superfamily that binds TRAIL and mediates apoptosis. The protein encoded by this gene is a member of the TNF-receptor superfamily, and contains an intracellular death domain. This receptor can be activated by tumor necrosis factor-related apoptosis inducing ligand (TNFSF10/TRAIL/APO-2L), and transduces apoptosis signal. Mice have a homologous gene, tnfrsf10b, that has been essential in the elucidation of the function of this gene in humans. Studies with FADD-deficient mice suggested that FADD, a death domain containing adaptor protein, is required for the apoptosis mediated by this protein. DR5 has been shown to interact with: Monoclonal antibodies targeting DR5 have been developed and are currently under clinical trials for patients suffer from a variety of cancer types, see Tigatuzumab (CS-1008). Luminescent iridium complex-peptide hybrids, serving as TRAIL mimics, have been designed, which target the death receptors DR4 and DR5 on cancer cells and induce their apoptosis. This article incorporates text from the United States National Library of Medicine, which is in the public domain.