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 4N7J
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Tailoring small molecules for an allosteric site on procaspase-6.
Murray, J., Giannetti, A.M., Steffek, M., Gibbons, P., Hearn, B.R., Cohen, F., Tam, C., Pozniak, C., Bravo, B., Lewcock, J., Jaishankar, P., Ly, C.Q., Zhao, X., Tang, Y., Chugha, P., Arkin, M.R., Flygare, J., Renslo, A.R.
Chemmedchem