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1f2h
From Proteopedia
(New page: 200px<br /> <applet load="1f2h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f2h" /> '''SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN...) |
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| - | [[Image:1f2h.gif|left|200px]]<br /> | + | [[Image:1f2h.gif|left|200px]]<br /><applet load="1f2h" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1f2h" size=" | + | |
caption="1f2h" /> | caption="1f2h" /> | ||
'''SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE TNFR1 ASSOCIATED PROTEIN, TRADD.'''<br /> | '''SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE TNFR1 ASSOCIATED PROTEIN, TRADD.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | TRADD is a multifunctional signaling adaptor protein that is recruited to | + | 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== | ==About this Structure== | ||
| - | 1F2H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1F2H is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Hsu, H.]] | [[Category: Hsu, H.]] | ||
| - | [[Category: Lin, L | + | [[Category: Lin, L L.]] |
[[Category: Malakian, K.]] | [[Category: Malakian, K.]] | ||
[[Category: McDonaugh, T.]] | [[Category: McDonaugh, T.]] | ||
| - | [[Category: Telliez, J | + | [[Category: Telliez, J B.]] |
[[Category: Tsao, D.]] | [[Category: Tsao, D.]] | ||
| - | [[Category: Xu, G | + | [[Category: Xu, G Y.]] |
[[Category: tnfr-1 associated protein]] | [[Category: tnfr-1 associated protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:03 2008'' |
Revision as of 10:34, 21 February 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
Page seeded by OCA on Thu Feb 21 12:34:03 2008
