Abstract
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.
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Acknowledgements
We thank Carlos F Ibanez for protein preparation and general support; Jason Y Tann for providing human ES cell cDNA; Chian Ming Low and Yoke Ping Cheong for assistance with sample purification; Jianfang Gao and Ket Yin Goh for technical support. This work was supported by grants from Tianjin University and Natural Science Foundation of Tianjin City (17JCYBJC24200).
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Zhang, N., Yuan, W., Fan, JS. et al. 1H, 15N and 13C chemical shift assignments of the C-terminal domain of TRADD. Biomol NMR Assign 11, 281–284 (2017). https://doi.org/10.1007/s12104-017-9763-6
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DOI: https://doi.org/10.1007/s12104-017-9763-6