1f2h

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2h OCA], [http://www.ebi.ac.uk/pdbsum/1f2h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f2h RCSB]</span>
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[[Category: tnfr-1 associated protein]]
[[Category: tnfr-1 associated protein]]
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Revision as of 17:14, 30 March 2008


PDB ID 1f2h

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Related: RELATED


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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


Overview

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.

About this Structure

1F2H is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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, Mol Cell. 2000 Jun;5(6):1051-7. PMID:10911999

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