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Poliovirus-encoded proteinase 3C: a possible evolutionary link between cellular serine and cysteine proteinase families
- Source :
- FEBS letters. 194(2)
- Publication Year :
- 1986
-
Abstract
- Here we demonstrate significant similarities between the amino acid sequences of trypsin (a serine protease) and the N-terminal piece of a specific fragment of the poliovirus polyprotein encompassing the sequence of the viral proteinase 3C, and also between cathepsin H (a cysteine protease) and the C-terminal piece of the same fragment. A coherent alignment of the sequences of the 3 proteases was obtained, in which the principal catalytically active residues occupy identical positions. A hypothesis is proposed that the viral enzyme may provide an evolutionary link between serine and cysteine protease families.
- Subjects :
- Proteases
Cathepsin H
Picornain 3C
viruses
Biophysics
Biology
Biochemistry
PTRPG, rat protrypsinogen. Amino acid residues are designated according to the one-letter code [1]
Cathepsin O
Structural Biology
Proteinase 3
Endopeptidases
Genetics
Animals
Trypsin
abr]PV, poliomyelitis virus (poliovirus)
Amino Acid Sequence
Molecular Biology
Serine protease
NS3
Serine Endopeptidases
Positive RNA virus
Cell Biology
DNA-Directed RNA Polymerases
Cat.H, rat cathepsin H
Cysteine protease
Biological Evolution
Cathepsins
Enzyme evolution
Rats
Cysteine Endopeptidases
Poliovirus
biology.protein
RNA, Viral
Cattle
TRP, bovine trypsin
MASP1
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 194
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- FEBS letters
- Accession number :
- edsair.doi.dedup.....7535e44bc1e4b7c1866374fbaf5fa3e5