CATH Classification

Domain Context

CATH Clusters

Superfamily 3.40.50.1460
Functional Family Caspase-3 preproprotein

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 4EJF
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Allosteric peptides bind a caspase zymogen and mediate caspase tetramerization.
Stanger, K., Steffek, M., Zhou, L., Pozniak, C.D., Quan, C., Franke, Y., Tom, J., Tam, C., Elliott, J.M., Lewcock, J.W., Zhang, Y., Murray, J., Hannoush, R.N.
Nat.Chem.Biol.