A signal of Fas-mediated apoptosis is transferred through an adaptor protein Fas-associated death domain protein (FADD) by interactions between the death domains of Fas and FADD. To understand the signal transduction mechanism of Fas-mediated apoptosis, we solved the solution structure of a murine FADD death domain. It consists of six helices arranged in a similar fold to the other death domains. 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, α2 of FADD with α3 of Fas and vice versa.
All Science Journal Classification (ASJC) codes
- Molecular Biology
- Cell Biology