Key result
Coxsackievirus 3C proteinase recognition of peptide substrates depends critically on the presence of the P2 phenylalanine and P4 alanine residues.
The P2 Phe and P4 Ala residues are important for the recognition and cleavage of peptide substrates by Coxsackievirus 3C proteinase.
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May guide 3C protease inhibitor design; leaves open in vivo relevance for coxsackievirus myocarditis.
Coxsackievirus 3C proteinase (3Cpro) cleaves between Gln and Gly, but additional amino acids are required to constitute a cleavage site. To investigate the additional sequence requirements, cleavages of the peptide substrate, and its derivatives were examined. Substitutions of each residue from the P2 to P5 positions showed the importance of the P2 Phe and P4 Ala for recognition by 3Cpro.
Miyashita et al. (1996) studied this question. Coxsackievirus 3C proteinase recognition of peptide substrates depends critically on the presence of the P2 phenylalanine and P4 alanine residues.
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