| Types | DnaRegion
|
| Roles | Protein_Domain
polypeptide_domain
|
| Sequences | BBa_K2124003_sequence (Version 1)
|
Description
This Serine protease is a component of Cerastes Cerastes (Desert Horned Viper) venom. It recognizes Thrombin cut sites in fibrinogen and upon cleavage converts the fibrinogen to fibrin monomers. The fibrin monomers can then link and begin clot formation in mammals. This part is polycistronic and also contains DsbC which is secreted to the periplasmic space. DsbC shuffles the Serine Protease disulfide bonds for proper folding and protein activity.
Notes
This Serine Protease protein is very small and stabilized by several disulfide bonds. The final construct is secreted into the periplasmic space with DsbC, a protein that shuffles disfulfide bonds. DsbC will allow the Serine Protease to fold properly with correct disulfide bonding. This will give stable functional protein. The DsbC gene is contained as part of this construct.
Source
Both the DsbC and Venom Serine Protease are from genomic sequence.
