Misplaced Pages

Sf caspase-1

Article snapshot taken from Wikipedia with creative commons attribution-sharealike license. Give it a read and then ask your questions in the chat. We can research this topic together.
Sf caspase-1
Sf caspase-1 structure by Ni et al. 2006
Identifiers
OrganismSpodoptera frugiperda (Fall armyworm)
SymbolN/A
PDB2NN3
RefSeq (mRNA)U81510.1
RefSeq (Prot)AAC47442.1
UniProtP89116
Search for
StructuresSwiss-model
DomainsInterPro

The protein Sf caspase-1 is the insect ortholog of the human effector caspases CASP3 (CPP32) and CASP7 (MCH3) in the species Spodoptera frugiperda (Fall armyworm). It was identified as the target of the baculoviral caspase inhibitor protein P35, which it cleaves and by which it is inhibited. Like other caspases, Sf caspase-1 is an aspartate-specific cysteine protease that is produced as an inactive proenzyme and becomes activated by autocatalytic cleavage. The Sf caspase-1 proenzyme is cleaved after the amino acid residues Asp-28 and Asp-195, resulting in a smaller 12 kDa fragment and a larger 19 kDa fragment. Just like with human caspases CASP3 or CASP7, the two cleavage fragments form heterodimers, which again form biologically active dimers-of-heterodimers consisting of two smaller and two larger fragments. Some experiments also showed cleavage of Sf caspase-1 at the residue Asp-184, resulting in an 18 kDa instead of 19 kDa fragment, however this result is likely an in vitro artefact. The insect immunophilin FKBP46 is a substrate of Sf caspase-1, which cleaves full length FKBP46 (~46 kDa) resulting in a ~25 kDa fragment.

References

  1. ^ Ahmad M, Srinivasula SM, Wang L, Litwack G, Fernandes-Alnemri T, Alnemri ES (January 1997). "Spodoptera frugiperda caspase-1, a novel insect death protease that cleaves the nuclear immunophilin FKBP46, is the target of the baculovirus antiapoptotic protein p35". The Journal of Biological Chemistry. 272 (3): 1421–4. doi:10.1074/jbc.272.3.1421. PMID 8999805.
  2. ^ Forsyth CM, Lemongello D, LaCount DJ, Friesen PD, Fisher AJ (February 2004). "Crystal structure of an invertebrate caspase". The Journal of Biological Chemistry. 279 (8): 7001–8. doi:10.1074/jbc.M312472200. PMID 14645217.
Proteases: cysteine proteases (EC 3.4.22)
Caspase
Fruit-derived
Calpain
Cathepsin
Other
Enzymes
Activity
Regulation
Classification
Kinetics
Types
Portal: Categories: