NMR structure and mutagenesis of the FADD (Mort1) death-effector domain

@article{Eberstadt1998NMRSA,  title={NMR structure and mutagenesis of the FADD (Mort1) death-effector domain},  author={Matthias Eberstadt and Baohua Huang and Zehan Chen and Robert P. Meadows and Shi Chung Ng and Lixin Zheng and Michael J. Lenardo and Stephen W. Fesik},  journal={Nature},  year={1998},  volume={392},  pages={941-945},  url={https://api.semanticscholar.org/CorpusID:4370202}}
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.

241 Citations

The three-dimensional solution structure and dynamic properties of the human FADD death domain.

The three-dimensional solution structure and characterised the internal polypeptide dynamics of human FADD-DD are determined and a pattern of increased rates of amide proton solvent exchange in the alpha3 helix correlates with a higher degree of solvent exposure for this secondary structure element.

Structural and biochemical analysis of the death domain complex formed at the Fas receptor

It was found that residues from many surface regions of Fas-DD are crucial for the FADD-DD interaction, which has potentially important implications for the nature of the organisation of the death domains in the death inducing signalling complex (DISC) formed at the Fas receptor.

Evidence of complex formation between FADD and c-FLIP death effector domains for the death inducing signaling complex

Evidence is provided indicating that the death effector domain (DED) of FADD interacts directly with the deathEffector domain of human c-FLIP, and homology modeling is used to develop a molecular docking model of Fadd and c- FLIP proteins.

Homotypic FADD interactions through a conserved RXDLL motif are required for death receptor-induced apoptosis

It is shown that FADD self-associates through a conserved RXDLL motif in the death effector domain (DED) and this suggests that lateral interactions among adapter molecules are required for death receptor apoptosis signaling and implicateSelf-association into oligomeric assemblies as a key function of death receptor adapter proteins in initiating apoptosis.

Full-length Fas-associated Death Domain Protein Interacts with Short Form of Cellular FLICE Inhibitory Protein

The purification and the characterization of human full-length FADD and c-FLIP S expressed in Escherichia coli are shown and the folding properties of the α-helical structure of Fadd and the super-secondary structure of c-FlIP S proteins were characterized by circular dichroism spectroscopy.

The Solution Structure of FADD Death Domain

The interactions between the death domains of Fas and FADD analyzed by site-directed mutagenesis indicate that charged residues in helices α2 and α3 are involved in death domain interactions, and the interacting helices appear to interact in anti-parallel pattern.
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27 References

NMR structure and mutagenesis of the Fas (APO-1/CD95) death domain

The solution structure of the Fas death domain, as determined by NMR spectroscopy, is described and the region of the death domain involved in self-association and binding to the downstream signalling partner FADD is identified.

CASH, a Novel Caspase Homologue with Death Effector Domains*

The findings suggest that CASH acts as an attenuator and/or initiator in CD95 and CD120a signaling for cell death, through a shared N-terminal sequence motif, the death effector domain.

NMR structure of the death domain of the p75 neurotrophin receptor

The nuclear magnetic resonance (NMR) structure of the 145 residue long p75ICD death domain may indicate a potential site of interaction with downstream targets, and unlike the death domains involved in signaling by the TNF receptor and Fas, p75 ICD does not self‐associate in solution.

RAIDD is a new 'death' adaptor molecule

An adaptor molecule, RAIDD, which has an unusual bipartite architecture comprising a carboxy-terminal death domain that binds to the homologous domain in RIP, indicating that the prodomain may, through homophilic interactions, determine the specificity of binding of ICE/CED-3 zymogens to regulatory adaptor molecules.

A Novel Protein That Interacts with the Death Domain of Fas/APO1 Contains a Sequence Motif Related to the Death Domain (*)

Induced expression of the cloned protein results in ligand-independent triggering of cytotoxicity, suggesting that it is involved in cell death induction by Fas/APO1.

Inhibition of death receptor signals by cellular FLIP

The characterization of an inhibitor of apoptosis is reported, designated FLIP (for FLICE-inhibitory protein), which is predominantly expressed in muscle and lymphoid tissues and may be implicated in tissue homeostasis as an important regulator of apoptotic regulation.

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