CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.50.1460
Functional Family Caspase-7

Enzyme Information

3.4.22.60
Caspase-7.
based on mapping to UniProt P55210
Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-.
-!- Caspase-7 is an effector/executioner caspase, as are caspase-3 (EC 3.4.22.56) and caspase-6 (EC 3.4.22.59). -!- 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. -!- Although a hydrophobic residue at P5 of caspase-2 (EC 3.4.22.55) and caspase-3 leads to more efficient hydrolysis, the amino-acid residue at this location in caspase-7 has no effect. -!- Caspase-7 is activated by the initiator caspases (caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63)). -!- Removal of the N-terminal prodomain occurs before cleavage in the linker region between the large and small subunits. -!- Belongs to peptidase family C14.

UniProtKB Entries (1)

P55210
CASP7_HUMAN
Homo sapiens
Caspase-7

PDB Structure

PDB 2QL9
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Plasticity of S2-S4 specificity pockets of executioner caspase-7 revealed by structural and kinetic analysis.
Agniswamy, J., Fang, B., Weber, I.T.
Febs J.