The picornaviral 3C proteinases: Cysteine nucleophiles in serine proteinase folds
Copyright policy )The picornaviral 3C proteinases: Cysteine nucleophiles in serine proteinase folds
AbstractThe 3C proteinases are a novel group of cysteine proteinases with a serine proteinase‐like fold that are responsible for the bulk of polyprotein processing in the Picornaviridae. Because members of this viral family are to blame for several ongoing global pandemic problems (rhinovirus, hepatitis A virus) as well as sporadic outbreaks of more serious pathologies (poliovirus), there has been continuing interest over the last two decades in the development of antiviral therapies. The recent determination of the structure of two of the 3C proteinases by X‐ray crystallography opens the door for the application of the latest advances in computer‐assisted identification and design of anti‐proteinase therapeutic/chemoprophylactic agents.
- University of Alberta Canada
Protein Folding, Binding Sites, Serine Endopeptidases, 3C Viral Proteases, Picornaviridae, Catalysis, Substrate Specificity, Cysteine Endopeptidases, Viral Proteins, Cysteine
Protein Folding, Binding Sites, Serine Endopeptidases, 3C Viral Proteases, Picornaviridae, Catalysis, Substrate Specificity, Cysteine Endopeptidases, Viral Proteins, Cysteine
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