The BioGRID | PUBLICATION VIEW

	Mol. Cell Jun (2000); 5(6):1051-7
Solution structure of N-TRADD and characterization of the interaction of N-TRADD and C-TRAF2, a key step in the TNFR1 signaling pathway.
Tsao DH, McDonagh T, Telliez JB, Hsu S, Malakian K, Xu GY, Lin LL
Musculoskeletal Science, Genetics Institute, Wyeth Research, Cambridge, Massachusetts 02140, USA. dtsao@genetics.com
Abstract: TRADD is a multifunctional signaling adaptor protein that is recruited to TNFR1 upon ligand binding. The C-terminal of TRADD comprises the "death domain" that is responsible for association of TNFR1 and other death domain-containing proteins such as FADD and RIP. The N-terminal domain (N-TRADD) promotes the recruitment of TRAF2 to TNFR1 by binding to the C-terminal of TRAF2, leading to the activation of JNK/AP1 and NF-kappa B. The solution structure of N-TRADD was determined, revealing a novel protein fold. A combination of NMR, BIAcore, and mutagenesis experiments was used to help identify the site of interaction of N-TRADD with C-TRAF2, providing a framework for future attempts to selectively inhibit the TNF signaling pathways.
[PUBMED: 10911999]