| Autor: |
Zhang, Ning, Yuan, Wensu, Fan, Jing-Song, Lin, Zhi |
| Zdroj: |
Biomolecular NMR Assignments; Oct2017, Vol. 11 Issue 2, p281-284, 4p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
|
Full text from SpringerLink