The structure of the key enzyme of foot-and-mouth disease has been deciphered

Recently, researchers reported that the determination of the complete structural map of the key replicase of foot-and-mouth disease will promote the development of new drugs that control this disease. By deciphering the structure of the 3C protease of the foot-and-mouth disease virus (FMDV) enzyme, researchers have taken a crucial step towards the development of protease inhibitors. The determination of this enzyme structure paves the way for understanding the details of the atoms of key viral enzymes that can act as drug targets. The function of the 3C protease is to help the virus self-replicate, so a drug that binds and inhibits the 3C protease will be able to interrupt its proliferation by preventing it from replicating and rendering it incapable of infecting herds. The structural details of this enzyme are published in the Journal of Biological Chemistry. Currently, researchers are designing molecules that can act as inhibitors. This enzyme consists of 213 amino acids and is folded into a typical protease form. The researchers spent four years cracking the structure of the enzyme. The most difficult problem in the study was the crystallization of this protease to facilitate X-ray crystal diffraction analysis. Researchers have identified the characteristics of the peptides recognized by the FMDV 3C protease, so they can now proceed with the study of inhibitors. The researchers figured out what the enzyme looked like, and the structure's identification provided information about what shapes and molecular types could specifically bind to this enzyme and inhibit its function.

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