Cleavage specificity of coxsackievirus 3C proteinase for peptide substrate (2): Importance of the P2 and P4 residues.
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
K
K
Central Research Laboratories, Maruishi Pharmaceutical Co., Ltd., Osaka, Japan.
Okunishi
J
J
Utsumi
R
R
Tagiri
S
S
Hotta
K
K
Komano
T
T
Tamura
T
T
Satoh
N
N
D000086042:3C Viral Proteases; D000409:Alanine / Q000737:chemistry; D003546:Cysteine Endopeptidases / Q000737:chemistry*; D005973:Glutamine / Q000737:chemistry*; D005998:Glycine / Q000737:chemistry*; D009842:Oligopeptides / Q000737:chemistry*; D010649:Phenylalanine / Q000737:chemistry; D013379:Substrate Specificity; D014764:Viral Proteins
D009842:Oligopeptides; D014764:Viral Proteins; D005973:Glutamine; D010649:Phenylalanine; D003546:Cysteine Endopeptidases; D000086042:3C Viral Proteases; D000409:Alanine; D005998:Glycine