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-1 |
Enzyme Information
| 3.4.22.36 |
Caspase-1.
based on mapping to UniProt P29466
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|-.
-!- Part of the family of inflammatory-caspases, which also includes caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. -!- Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. -!- Cleaves pro-interleukin-1-beta (pro-IL-1-beta) to form mature IL-1- beta, a potent mediator of inflammation. -!- Also activates the proinflammatory cytokine, IL-18, which is also known as interferon-gamma-inducing factor. -!- Inhibited by Ac-Tyr-Val-Ala-Asp-CHO. -!- Caspase-11 plays a critical role in the activation of caspase-1 in mice whereas caspase-4 enhances its activation in humans. -!- Belongs to peptidase family C14.
|
UniProtKB Entries (1)
| P29466 |
CASP1_HUMAN
Homo sapiens
Caspase-1
|
PDB Structure
| PDB | 1BMQ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Peptide based interleukin-1 beta converting enzyme (ICE) inhibitors: synthesis, structure activity relationships and crystallographic study of the ICE-inhibitor complex.
Chem.Pharm.Bull.
|
