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Members of the death receptor family play a prominent role in developmental and pathological neuronal cell death. The death signal is transduced via interaction between the death domain of the receptor and an intracellular adapter, TRADD. We performed alanine-scanning mutagenesis of specific charged residues in the TR3 death domain to determine whether they play a crucial role in TR3-TR3 and TR3-TRADD interaction. Mutation of charged residues in the second and third helices of the TR3 death domain failed to perturb self-interaction or interaction with TRADD. These data suggest that despite some similarity between the death domains of TR3 and TNFR1 the nature of the interaction with TRADD differs from that reported for TNFR1.

Type

Journal article

Journal

Protein Eng

Publication Date

10/2002

Volume

15

Pages

811 - 815

Keywords

Alanine, Amino Acid Sequence, Amino Acid Substitution, Amino Acids, Acidic, Amino Acids, Basic, Animals, DNA Primers, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Precipitin Tests, Protein Structure, Tertiary, Proteins, Receptors, Tumor Necrosis Factor, Saccharomyces cerevisiae, Solvents, TNF Receptor-Associated Factor 1, Two-Hybrid System Techniques