1H, 15N and 13C chemical shift assignments of the C-terminal domain of TRADD

The tumor necrosis factor receptor-associated death domain protein, TRADD, is a multifunctional intracellular molecule participating in divergent signaling pathways, such as NF-kappa B and apoptosis. TRADD consists of two structurally distinct domains. Its N-terminal domain displays an alpha-beta 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 p75(NTR)-mediated signalling in MCF-7 human breast cancer cells. Here we report backbone and sidechain H-1, C-13 and N-15 chemical shift assignments of TRADD DD in pure water as a basis for further structural and functional studies.