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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 34, Number 4
BKCSDE 34(4)
April 20, 2013 

Overexpression and Biological Characterization of the Death Domain Complex between TRADD and FADD
Eun Young Hwang, Mi Suk Jeong, Minkyung Sung, Se Bok Jang*
Soluble expression, TRADD, FADD, Interaction
The tumor necrosis factor-receptor 1 (TNFR1)-associated death domain protein (TRADD) contains an Nterminal TRAF binding domain and a C-terminal death domain. TRADD is known to interact directly with TNF receptor 2 (TNFR2) and the Fas-associated death domain protein (FADD), which are signal transducers that activate NF-kB and induce apoptosis, respectively. To date, there has been no structural information on the TRADD and FADD death domain (DDs) complex. In this study, the death domains of TRADD and FADD were co-expressed and purified from Escherichia coli for structural characterization. We found that human TRADD (hTRADD) interacted strongly with mouse FADD (mFADD) via their DDs and interacted weakly with human FADD (hFADD)-DD. Moreover, the structures of the TRADD-DD:FADD-DD complexes were separately modeled from predicted structures in the protein data bank (PDB). The results of this study will have important applications in human diseases such as cancer, AIDS, degenerative and autoimmune diseases, and infectious diseases.
1089 - 1095
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