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3/28/2025, 10:25:26 AM UTC
Commit: 461ca8d8fe5b1efd4c01fc87e5b5eb592e2d154a
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Death Protein Domain

Apoptosis: Death Domain

The Death domain from FADD.

Domain Binding and Function

Death domains (DD) are 80–100 residue long motifs involved in apoptotic signal transduction. They are found in both cytoplasmic proteins and in transmembrane proteins, including members of the tumor necrosis factor receptor superfamily. Death domains serve as recruiting modules as they are able 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 may arise primarily through electrostatic interactions. Binding is specific and is thought to arise through complementary charge patterns on dimerization partners.

Structure Reference

  1. Jeong, E.-J. et al. (1999) J. Biol. Chem. 274(23), 16337–16342.

Examples of Domain Proteins

Apoptosis: Death Domain

Binding Examples

TNF Receptors

Adaptors

Adaptors

Adaptors

Fas, TRAIL R1

FADD

RIP

TRADD

Fas

RIP

RIP

RAIDD

TNF-R55

TRADD

TRADD

FADD