1f2h: Difference between revisions
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[[Image:1f2h.gif|left|200px]] | [[Image:1f2h.gif|left|200px]] | ||
'''SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE TNFR1 ASSOCIATED PROTEIN, TRADD.''' | {{Structure | ||
|PDB= 1f2h |SIZE=350|CAPTION= <scene name='initialview01'>1f2h</scene> | |||
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'''SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE TNFR1 ASSOCIATED PROTEIN, TRADD.''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1F2H is a [ | 1F2H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2H OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10911999 10911999] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tnfr-1 associated protein]] | [[Category: tnfr-1 associated protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:03:28 2008'' | ||
Revision as of 09:03, 20 March 2008
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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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