Article
Mutational analysis of the putative substrate-binding site of 3C proteinase of coxsackievirus B3.
Bioscience, biotechnology, and biochemistry - 1 Jan 1995
Miyashita K, Utsumi R, Utsumi T, Komano T, Satoh N
Abstract excerpt
Single amino acid substitutions were introduced into the putative substrate-binding site of 3C proteinase (3Cpro) of coxsackievirus B3, a member of the picornavirus family. Mutations at either Thr142, His161, Gly164, Gly169, or Ala172 severely impaired or abolished the proteolytic activity except that a conservative Thr142 to Ser mutant had detectable activity. These results, which have shown the participation of...
Topics
- Alanine
- Amino Acid Sequence
- Base Sequence
- Binding Sites
- Conserved Sequence
- DNA Primers
- Electrophoresis, Polyacrylamide Gel
- Endopeptidases
- Enterovirus B, Human
- Escherichia coli
- Glycine