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 | Caspase 9 |
Enzyme Information
| 3.4.22.62 |
Caspase-9.
based on mapping to UniProt P55211
Strict requirement for an Asp residue at position P1 and with a marked preference for His at position P2. It has a preferred cleavage sequence of Leu-Gly-His-Asp-|-Xaa.
-!- Caspase-9 is an initiator caspase, as are caspase-2 (EC 3.4.22.55), caspase-8 (EC 3.4.22.61) and caspase-10 (EC 3.4.22.63). -!- Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. -!- An alternatively spliced version of caspase-9 also exists, caspase- 9S, that inhibits apoptosis, similar to the situation found with caspase-2. -!- Phosphorylation of caspase-9 from some species by Akt, a serine- threonine protein kinase, inhibits caspase activity in vitro and caspase activation in vivo. -!- The activity of caspase-9 is increased dramatically upon association with the apoptosome but the enzyme can be activated without proteolytic cleavage. -!- Procaspase-3 is the enzyme's physiological substrate. -!- Belongs to peptidase family C14.
|
UniProtKB Entries (1)
| P55211 |
CASP9_HUMAN
Homo sapiens
Caspase-9
|
PDB Structure
| PDB | 1JXQ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Dimer formation drives the activation of the cell death protease caspase 9.
Proc.Natl.Acad.Sci.USA
|