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Eberstadt, M, Huang, B, Chen, Z, Meadows, RP, Ng, SC, Zheng, L, Lenardo, MJ and Fesik, SW (1998) NMR structure and mutagenesis of the FADD (Mort1) death-effector domain. Nature 392:941-5
When activated, membrane-bound receptors for Fas and tumour-necrosis factor initiate programmed cell death by recruiting the death domain of the adaptor protein FADD to the membrane. FADD then activates caspase 8 (also known as FLICE or MACH) through an interaction between the death-effector domains of FADD and caspase 8. This ultimately leads to the apoptotic response. Death-effector domains and homologous protein modules known as caspase-recruitment domains have been found in several proteins and are important regulators of caspase (FLICE) activity and of apoptosis. Here we describe the solution structure of a soluble, biologically active mutant of the FADD death-effector domain. The structure consists of six antiparallel, amphipathic alpha-helices and resembles the overall fold of the death domains of Fas and p75. Despite this structural similarity, mutations that inhibit protein-protein interactions involving the Fas death domain have no effect when introduced into the FADD death-effector domain. Instead, a hydrophobic region of the FADD death-effector domain that is not present in the death domains is vital for binding to FLICE and for apoptotic activity.
Adaptor Proteins, Signal Transducing; Amino Acid Sequence; Antigens, CD95/chemistry; Apoptosis; Carrier Proteins/chemistry; Carrier Proteins/genetics; Carrier Proteins/metabolism; Caspase 8; Caspase 9; Caspases; Crystallography, X-Ray; Cysteine Endopeptidases/chemistry; Cysteine Endopeptidases/metabolism; Fas-Associated Death Domain Protein; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Protein Folding; Protein Structure, Secondary
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Analysis from FIgure 1 Northern blotting, and Figure 3 Sequence Alignment
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