Abstract
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.
Original language | English |
---|---|
Pages (from-to) | 16337-16342 |
Number of pages | 6 |
Journal | Journal of Biological Chemistry |
Volume | 274 |
Issue number | 23 |
DOIs | |
Publication status | Published - 1999 Jun 4 |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Cell Biology