Zhang Ning, Yuan Wensu, Fan Jing-Song, Lin Zhi
School of Life Sciences, Tianjin University, Tianjin, 300072, People's Republic of China.
Department of Biological Sciences, National University of Singapore, Singapore, 117543, Singapore.
Biomol NMR Assign. 2017 Oct;11(2):281-284. doi: 10.1007/s12104-017-9763-6. Epub 2017 Aug 16.
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 p75-mediated signalling in MCF-7 human breast cancer cells. Here we report backbone and sidechain H, C and N chemical shift assignments of TRADD DD in pure water as a basis for further structural and functional studies.
肿瘤坏死因子受体相关死亡结构域蛋白（TRADD）是一种多功能细胞内分子，参与多种信号通路，如核因子κB（NF-κB）和凋亡通路。TRADD由两个结构不同的结构域组成。其N端结构域呈现α-β折叠结构，而C端结构域属于死亡结构域（DD）超家族。TRADD DD是肿瘤坏死因子受体1信号传导的核心成分。它通过同型相互作用与其他含DD的蛋白质相互作用。TRADD DD还参与MCF-7人乳腺癌细胞中p75介导的信号传导。在此，我们报告了纯水中TRADD DD的主链和侧链H、C和N化学位移归属，作为进一步进行结构和功能研究的基础。
