HRV-3C Protease has been used to remove the GST tag from the DsCystatin protein.
HRV3C Protease has a therapeutic implication because of its unique protein structure. It may be used for the biochemical and structural characterization conducted on HRV 3C protease along with the development of 3C protease inhibitors.
HRV3C Protease is a recombinant restriction-grade cysteine protease. It folds into two topologically alike six-stranded β barrels. However, β barrels are different in length and individual position as well as in loops connecting elements of secondary structure. The protease is distinguishable from others by the fact that it has a cysteine nucleophile but with a chymotrypsin-like serine protease folding.
Human rhinovirus 3C protease (HRV3C Protease) is a cysteine protease that recognizes the cleavage site of Leu-Glu-Val-Leu-Phe-Gln*Gly-Pro. It is supplied as a 47 kDa protein with both GST and Histidine tags for easy removal by His-Select or Glutathione agarose along with the cleaved tag. HRV3C Protease is capable of cleaving small peptides with the sequence of polyprotein processing sites. It cleaves after the glutamine residue. HRV cleavage site generally contains Gln/Gly scissile bond.
