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
| 3.4.22.59 |
Caspase-6.
based on mapping to UniProt P55212
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Val-Glu-His-Asp-|-.
-!- Caspase-6 is an effector/executioner caspase, as are caspase-3 (EC 3.4.22.56) 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 lead to the apoptotic phenotype. -!- Caspase-6 can cleave its prodomain to produce mature caspase-6, which directly activates caspase-8 (EC 3.4.22.61) and leads to cytochrome c release from the mitochondria; the release of cytochrome c, which is an essential component of the intrinsic apoptosis pathway. -!- Can also cleave and inactivate lamins, the intermediate filament scaffold proteins of the nuclear envelope, leading to nuclear fragementation in the final phases of apoptosis. -!- Belongs to peptidase family C14.
|
UniProtKB Entries (1)
| P55212 |
CASP6_HUMAN
Homo sapiens
Caspase-6
|
PDB Structure
| PDB | 3QNW |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure of human caspase-6 in complex with Z-VAD-FMK: New peptide binding mode observed for the non-canonical caspase conformation.
Bioorg.Med.Chem.Lett.
|