The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD.
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.
Jeong
E J
EJ
Structural Biology Center, Korea Institute of Science and Technology, Seoul, 130-650, Korea University, Seoul, 136-701, Korea.
Bang
S
S
Lee
T H
TH
Park
Y I
YI
Sim
W S
WS
Kim
K S
KS
D048868:Adaptor Proteins, Signal Transducing; D000595:Amino Acid Sequence; D000818:Animals; D017209:Apoptosis; D001665:Binding Sites; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism*; D053200:Fas-Associated Death Domain Protein; D006801:Humans; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D016415:Sequence Alignment; D012996:Solutions; D013329:Structure-Activity Relationship; D019014:fas Receptor / Q000378:metabolism*
D048868:Adaptor Proteins, Signal Transducing; D002352:Carrier Proteins; C505533:FADD protein, human; C505534:Fadd protein, mouse; D053200:Fas-Associated Death Domain Protein; D010446:Peptide Fragments; D012996:Solutions; D019014:fas Receptor