The tumor necrosis factor receptor-associated death domain protein, TRADD, is a multifunctional intracellular molecule participating in divergent signaling pathways, such as NF-κB and apoptosis. TRADD consists of two structurally distinct domains. Its N-terminal domain displays an α-β plaits fold while its C-terminal domain belongs to the death domain (DD) superfamily. TRADD DD is a central component in the tumor necrosis factor receptor 1 signaling. It interacts with other DD-containing proteins through homotypic interactions. TRADD DD is also involved in p75NTR-mediated signalling in MCF-7 human breast cancer cells. Here we report backbone and sidechain 1H, 13C and 15N chemical shift assignments of TRADD DD in pure water as a basis for further structural and functional studies.
Keywords: Assignment; DD; NMR; TRADD.