Poliovirus‐encoded proteinase 3C: a possible evolutionary link between cellular serine and cysteine proteinase families

@article{Gorbalenya1986PoliovirusencodedP3,
  title={Poliovirus‐encoded proteinase 3C: a possible evolutionary link between cellular serine and cysteine proteinase families},
  author={Alexander E. Gorbalenya and Vladimir M. Blinov and Alexei P. Donchenko},
  journal={FEBS Letters},
  year={1986},
  volume={194}
}
Chimeric picornavirus polyproteins demonstrate a common 3C proteinase substrate specificity
TLDR
Cross-species proteolytic processing was demonstrated by the 3C proteinases of human rhinovirus 14 and coxsackievirus B3 on poliovirus-specific polypeptide precursors, providing evidence for the existence of common conformational determinants necessary for 3C-mediated processing.
The picornaviral 3C proteinases: Cysteine nucleophiles in serine proteinase folds
  • B. Malcolm
  • Biology, Chemistry
    Protein science : a publication of the Protein Society
  • 1995
TLDR
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.
Viral cysteine proteinases
TLDR
Dozens of novel cysteine proteinases have been identified in positive single-STRanded RNA viruses and, for the first time, in large double-stranded DNA viruses, indicating direct descendants of primordial proteolytic enzymes.
Identification of a trypsin-like serine proteinase domain encoded by ORF 1a of the coronavirus IBV.
TLDR
Avian infectious bronchitis virus is the prototype species of the Coronaviridae, a family of enveloped viruses with large positive-stranded RNA genomes and three of these encode the major virion structural proteins spike, membrane, and nucleocapsid.
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