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
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Jeong, E. J., Bang, S. H., Lee, T. H., Park, Y. I., Sim, W. S., & Kim, K. S. (1999). The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD. Journal of Biological Chemistry, 274(23), 16337-16342. https://doi.org/10.1074/jbc.274.23.16337