FMDV 3C.
The viral RNA genome is translated as a single polypeptide precursor that must be cleaved into functional proteins by virally encoded proteases. The highly conserved FMDV 3C protease is responsible for 10 out of the 13 cleavages, making the enzyme an attractive target for antiviral drugs. The 3C protease cuts itself out of the polyprotein and is responsible for processing the P1 peptide (with exception of VP4-VP21 (1AB) as well as P2 and P3, which lead to its categorization as a catalytic triad. The kinetics of processing proceeds to cleave the bonds in this order of preference: VP3-VP1, VP0-VP3, and VP1-2A where they then assemble into a triangular protomer. Five protomers come together to make pentamers, twelve of which conjoin to complete the virus shell.
Function
Disease
Relevance
Structural highlights
Click " " to view by Group, and another to make of the protein.
