1F2H

SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE TNFR1 ASSOCIATED PROTEIN, TRADD.

Summary for 1F2H

• Entry DOI: 10.2210/pdb1f2h/pdb
• NMR Information: BMRB: 4636
• Descriptor: TUMOR NECROSIS FACTOR RECEPTOR TYPE 1 ASSOCIATED DEATH DOMAIN PROTEIN (1 entity in total)
• Functional Keywords: tnfr-1 associated protein, apoptosis
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 18572.16

Authors

Tsao, D.,McDonaugh, T.,Malakian, K.,Xu, G.-Y.,Telliez, J.-B.,Hsu, H.,Lin, L.-L. (deposition date: 2000-05-24, release date: 2001-05-30, Last modification date: 2024-05-22)

Primary citation

Tsao, D.H.,McDonagh, T.,Telliez, J.B.,Hsu, S.,Malakian, K.,Xu, G.Y.,Lin, L.L.
Solution structure of N-TRADD and characterization of the interaction of N-TRADD and C-TRAF2, a key step in the TNFR1 signaling pathway.
Mol.Cell, 5:1051-1057, 2000

PubMed 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
DOI: 10.1016/S1097-2765(00)80270-1

Experimental method

SOLUTION NMR