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 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Cell Biology
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}
The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD. / Jeong, Eui Jun; Bang, Sook Hee; Lee, Tae Ho; Park, Young In; Sim, Woong Seop; Kim, Key Sun.
In: Journal of Biological Chemistry, Vol. 274, No. 23, 04.06.1999, p. 16337-16342.Research output: Contribution to journal › Article
TY - JOUR
T1 - The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD
AU - Jeong, Eui Jun
AU - Bang, Sook Hee
AU - Lee, Tae Ho
AU - Park, Young In
AU - Sim, Woong Seop
AU - Kim, Key Sun
PY - 1999/6/4
Y1 - 1999/6/4
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0033522889&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033522889&partnerID=8YFLogxK
U2 - 10.1074/jbc.274.23.16337
DO - 10.1074/jbc.274.23.16337
M3 - Article
C2 - 10347191
AN - SCOPUS:0033522889
VL - 274
SP - 16337
EP - 16342
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 23
ER -