Structural and mechanistic aspects of 3C proteases from the Picornavirus family.
Picornavirus 3C proteases are prime targets for rational drug design. This viral protease appears in a large number of viruses from the Picornavirus family that cause serious disease syndromes, and it has an important role in the life cycle of the virus, processing the translation product of the Picornavirus genome by progressive co- and posttranslational cleavages. It is, therefore, important to gain structural and mechanistic information about this family of enzymes. We concentrate in this paper on the specific features of the 3C; particularly, we are trying to show that the 3C constitute a new family to enzymes which is neither a serine- nor a cysteine-type protease. General basic theory on the behavior of sulfur nucleophile vs the behavior of oxygen nucleophile regarding the nucleophilic attack on carbonyl compounds and the possible determinants in the structure of 3C viral proteases of rhinovirus 1A are being discussed.
Arad
D
D
Department of Microbiology and Biotechnology, Tel-Aviv University, Ramat-Aviv, Israel.
Kreisberg
R
R
Shokhen
M
M
D000086042:3C Viral Proteases; D003545:Cysteine / Q000737:chemistry; D003546:Cysteine Endopeptidases / Q000737:chemistry*; D008958:Models, Molecular; D010849:Picornaviridae / Q000201:enzymology*; D011480:Protease Inhibitors / Q000494:pharmacology; D011487:Protein Conformation; D011789:Quantum Theory; D017386:Sequence Homology, Amino Acid; D012694:Serine / Q000737:chemistry; D012984:Software; D013329:Structure-Activity Relationship; D013455:Sulfur / Q000737:chemistry; D014764:Viral Proteins
D011480:Protease Inhibitors; D014764:Viral Proteins; D012694:Serine; D013455:Sulfur; D003546:Cysteine Endopeptidases; D000086042:3C Viral Proteases; D003545:Cysteine