TRADD, N-terminal domain superfamily

SCOP classification

• Root: SCOP hierarchy in SUPERFAMILY [ 0] (11)
• Class: Alpha and beta proteins (a+b) [ 53931] (376)
• Fold: Ferredoxin-like [ 54861] (59)
• Superfamily: TRADD, N-terminal domain [ 55044]
• Families: TRADD, N-terminal domain [ 55045]

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Superfamily statistics

	Genomes (60)	Uniprot 2018_03 genome	PDB chains (SCOP 1.75)
Domains	73	174	2
Proteins	72	173	2

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Functional annotation

• General category: Regulation
• Detailed category: Signal transduction

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InterPro annotation

• Cross references: IPR009095 SSF55044 Protein matches
• Abstract:

  TRADD is a signalling adaptor protein involved in tumour necrosis factor-receptor I (TNFR1)-associated apoptosis and cell survival. The decision between apoptosis and cell survival involves the interplay between two sequential signalling complexes. The plasma membrane-bound complex I is comprised of TNFR1, TRADD, the kinase RIP1, and TRAF2, which together mediate the activation of NF-kappaB. Subsequently, complex II is formed in the cytoplasm, where TRADD and RIP1 associate with FADD and caspase-8. If NF-kappaB is activated by complex I, then complex II will associate with the caspase-8 inhibitor FLIP(L) and the cell survives, while the failure to activate NF-kappaB leads to apoptosis [12887920].

  The TRADD C-terminal death domain is responsible for its association with TNFR1, and with the death-domain proteins FADD and RIP1, which promote apoptosis. The TRADD N-terminal domain binds TRAF2 and promotes TRAF2 recruitment to TNFR1, thereby mediating the activation of NK-kappaB and JNK/AP1, which promote cell survival [10911999]. The N-terminal TRADD domain is composed of an alpha-beta sandwich, where the beta strands form an antiparallel beta-sheet.

InterPro database

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