Abstract
Picornaviruses are a family of viruses which belong to the large group of positive-sense, single-stranded RNA viruses (RUECKERT 1996). It was realized 30 years ago that the product of the translation of the RNA genome of these viruses is proteolytically processed to yield the mature viral proteins (SUMMERS) and (MAIZEL 1968; KORANT 1972). Subsequently, it could be shown for two different picornaviruses that the processing enzyme is a specific, virally encoded proteinase (PELHAM 1978; GORBALENYA et al. 1979; KORANT et al. 1979; PALMENBERG et al. 1979). Once the amino-acid sequences of the viral proteinases became available, predictions were made concerning the structure of the picornaviral 3C proteinases (GROBALENYA et al. 1986; BAZAN and FLETTERICK 1988; GORBALENYA et al. 1989). These predictions were remarkable. Based on an analysis of several conserved sequence motifs within the amino-acid sequence of the 3C proteinases, it was suggested that these proteinases are structurally related to the chymotrypsin-like proteinases but with a cysteine residue as the active-site nucleophile. Crystal structures of 3C proteinases from two picornaviruses confirmed this prediction (ALLAIRE et al. 1994; MATTHEWS et al. 1994). At present, crystal structures of 3C proteinases from viruses, belonging to three different genera of the picornaviruses, have been published (MATTHEWS et al. 1994; BERGMANN et al. 1997; MOSIMANN et al. 1997).
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Bergmann, E.M., James, M.N.G. (2000). The 3C Proteinases of Picornaviruses and Other Positive-Sense, Single-Stranded RNA Viruses. In: von der Helm, K., Korant, B.D., Cheronis, J.C. (eds) Proteases as Targets for Therapy. Handbook of Experimental Pharmacology, vol 140. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-57092-6_7
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