CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.70 | Alpha-Beta Plaits |
|
3.30.70.1470 | Caspase-like |
Domain Context
CATH Clusters
| Superfamily | Caspase-like |
| Functional Family | Caspase-3 |
Enzyme Information
| 3.4.22.56 |
Caspase-3.
based on mapping to UniProt P42574
Strict requirement for an Asp residue at positions P1 and P4. It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid residue at P3, although Val or Ala are also accepted at this position.
-!- Caspase-3 is an effector/executioner caspase, as are caspase-6 (EC 3.4.22.59) and caspase-7 (EC 3.4.22.60). -!- These caspases are responsible for the proteolysis of the majority of cellular polypeptides, (e.g. poly(ADP-ribose) polymerase (PARP)), which leads to the apoptotic phenotype. -!- Procaspase-3 can be activated by caspase-1 (EC 3.4.22.36), caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63) as well as by the serine protease granzyme B. -!- Caspase-3 can activate procaspase-2 (EC 3.4.22.55). -!- Activation occurs by inter-domain cleavage followed by removal of the N-terminal prodomain. -!- While Asp-Glu-(Val/Ile)-Asp is thought to be the preferred cleavage sequence, the enzyme can accommodate different residues at P2 and P3 of the substrate. -!- Like caspase-2, a hydrophobic residue at P5 of caspase-3 leads to more efficient hydrolysis, e.g. (Val/Leu)-Asp-Val-Ala-Asp-|- is a better substrate than Asp-Val-Ala-Asp-|-. -!- This is not the case for caspase-7. -!- Belongs to peptidase family C14.
|
UniProtKB Entries (1)
| P42574 |
CASP3_HUMAN
Homo sapiens
Caspase-3
|
PDB Structure
| PDB | 6BG0 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Modifications to a common phosphorylation network provide individualized control in caspases.
J. Biol. Chem.
|
