Detection of a trypsin-like serine protease domain in flaviviruses and pestiviruses.
We propose through a sequence and structural-pattern analysis that a protein domain of undefined function encoded by the enveloped RNA flavi- and pestivruses is a Ser active-center enzyme related to the cellular trypsin family. A further homology is emphasized with the group of (Cys active-center) viral proteases encoded by nonenveloped RNA viruses of the picorna-, como-, nepo-, and potyvirus classes. Structural modeling of the putative flaviviral protease domain suggests amino acids that are crucial for catalytic activity and substrate binding.
Bazan
J F
JF
Department of Biophysics, University of California, Berkeley 94720.
Fletterick
R J
RJ
D000595:Amino Acid Sequence; D005416:Flavivirus / Q000201:enzymology / Q000235:genetics*; D008969:Molecular Sequence Data; D010576:Pestivirus / Q000201:enzymology / Q000235:genetics*; D012697:Serine Endopeptidases / Q000235:genetics*; D014764:Viral Proteins / Q000235:genetics / Q000648:ultrastructure
D014764:Viral Proteins; D012697:Serine Endopeptidases