| First Author | Jeong EJ | Year | 1999 |
| Journal | J Biol Chem | Volume | 274 |
| Issue | 23 | Pages | 16337-42 |
| PubMed ID | 10347191 | Mgi Jnum | J:55358 |
| Mgi Id | MGI:1337852 | Doi | 10.1074/jbc.274.23.16337 |
| Citation | Jeong EJ, et al. (1999) The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD. J Biol Chem 274(23):16337-42 |
| abstractText | 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 alpha2 and alpha3 are involved in death domain interactions, and the interacting helices appear to interact in anti-parallel pattern, alpha2 of FADD with alpha3 of Fas and vice versa. |
