J Biol Chem. 1999 Jun 4;274(23):16337-42.

The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD.External

Jeong, E. J., Bang, S., Lee, T. H., Park, Y. I., Sim, W. S., Kim, K. S.,
--- - Structural Biology Center, Korea Institute of Science and Technology, Seoul, 130-650, Korea University, Seoul, 136-701, Korea.
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.
PMID: 10347191External
Arrow2 In vitro interaction Arrow2 In vivo interaction Arrow2 Characterization Arrow2 Functional role Arrow2 top
In vitro interaction
  DD1 DD2 Reference
Family DD1 DD2 Method Species Region Expression Species Region Expression
DD FADD Link Fas In vitro purification protein assembly(Surface plasmon resonance) Not specified 89-183 E.coli Human Not specified E.coli 10347191
(Link: click this icon to show interactions only between the two corresponding DDs)
Arrow2 In vitro interaction Arrow2 In vivo interaction Arrow2 Characterization Arrow2 Functional role Arrow2 top
Characterization
  Stoichiometry Affinity Protein-Protein interface Reference
Family DD1 DD2 Method Mutation Complex structure
DD FADD Link Fas Surface plasmon resonance 1.0E+07M-1 R110A, R113A, R117A, E118A, V121N, E123A (FADD) 10347191
(Link: click this icon to show interactions only between the two corresponding DDs)