Apoptosis: Death Domain
The Death domain from FADD.
Domain Binding and Function
Death domains (DD) are 80–100 residues long motifs involved in apoptotic signal transduction. They are found both in cytoplasmic proteins and in transmembrane proteins including members of the tumor necrosis factor receptor superfamily. Death domains serve as recruiting modules through their ability to heterodimerize with the death domains of distinct proteins, including adaptor proteins such as FADD. Due to the significant polarization of charged residues on the surface of the death domain, dimerization is believed to arise primarily through electrostatic interactions. Binding has been shown to be specific and is thought to arise through complementary charge patterns on dimerization partners.
Structure Reference
- Jeong, E.-J. et al. (1999) J. Biol. Chem. 274(23), 16337–16342.
Examples of Domain Proteins
Binding Examples
| TNF Receptors | Adaptors | Adaptors | Adaptors |
|---|---|---|---|
| Fas, TRAIL R1 | FADD | RIP | TRADD |
| Fas | RIP | RIP | RAIDD |
| TNF-R55 | TRADD | TRADD | FADD |
