CATH Classification

Domain Context

CATH Clusters

Superfamily Caspase-like
Functional Family

Enzyme Information
based on mapping to UniProt Q14790
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-(Gly/Ser/Ala).
-!- Caspase-8 is an initiator caspase, as are caspase-2 (EC, caspase-9 (EC and caspase-10 (EC -!- Apical activator of the extrinsic (death receptor) apoptosis pathway, triggered by death receptor ligation. -!- Contains two tandem death effector domains (DEDs) in its N-terminal prodomain, which play a role in procaspase activation. -!- Linked to cell surface death receptors such as Fas. -!- When Fas is aggregated by the Fas ligand, procaspase-8 is recruited to the death receptor where it is activated. -!- Has a preference for Glu at P3 and prefers small residues, such as Gly, Ser and Ala at the P1' position. -!- Has very broad P4 specificity, tolerating substrates with Asp, Val or Leu in this position. -!- Endogenous substrates for caspase-8 include procaspase-3, the pro- apoptotic Bcl-2 family member Bid, RIP, PAK2 and the caspase-8 activity modulator FLIP(L). -!- Belongs to peptidase family C14.

UniProtKB Entries (1)

Homo sapiens

PDB Structure

External Links
Organism Escherichia
Primary Citation
The atomic-resolution structure of human caspase-8, a key activator of apoptosis.
Watt, W., Koeplinger, K.A., Mildner, A.M., Heinrikson, R.L., Tomasselli, A.G., Watenpaugh, K.D.
Structure Fold.Des.