1f2h

<StructureSection load='1f2h' size='340' side='right'caption='[[1f2h]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1f2h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F2H FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1f2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2h OCA], [https://pdbe.org/1f2h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f2h RCSB], [https://www.ebi.ac.uk/pdbsum/1f2h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f2h ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/TRADD_HUMAN TRADD_HUMAN]] The nuclear form acts as a tumor suppressor by preventing ubiquitination and degradation of isoform p19ARF/ARF of CDKN2A by TRIP12: acts by interacting with TRIP12, leading to disrupt interaction between TRIP12 and isoform p19ARF/ARF of CDKN2A (By similarity). Adapter molecule for TNFRSF1A/TNFR1 that specifically associates with the cytoplasmic domain of activated TNFRSF1A/TNFR1 mediating its interaction with FADD. Overexpression of TRADD leads to two major TNF-induced responses, apoptosis and activation of NF-kappa-B.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:10911999</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1f2h" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Human]]

[[Category: Hsu, H]]

[[Category: Lin, L L]]

[[Category: Malakian, K]]

[[Category: McDonaugh, T]]

[[Category: Telliez, J B]]

[[Category: Tsao, D]]

[[Category: Xu, G Y]]

[[Category: Tnfr-1 associated protein]]