CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.1460 |
Domain Context
CATH Clusters
| Superfamily | 3.40.50.1460 |
| Functional Family |
Enzyme Information
| 3.4.22.61 |
Caspase-8.
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 3.4.22.55), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63). -!- 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)
| Q14790 |
CASP8_HUMAN
Homo sapiens
Caspase-8
|
PDB Structure
| PDB | 2C2Z |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Design, Synthesis, and Evaluation of Aza-Peptide Michael Acceptors as Selective and Potent Inhibitors of Caspases-2, -3, -6, -7, -8, -9, and - 10.
J.Med.Chem.
|
