Structural analysis of foot-and-mouth disease virus 3C protease: a viable target for antiviral drugs?
Foot-and-mouth disease virus causes a major global agricultural problem that is difficult to control with existing vaccines. Structural analyses of the viral 3C protease not only have provided fresh insights into the catalytic mechanism of an unusual class of chymotrypsin-like cysteine proteases, but also are generating valuable information to drive the quest for effective antiviral therapies.
Curry
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Biophysics Section, Division of Cell and Molecular Biology, Blackett Laboratory, Imperial College, Exhibition Road, London SW7 2AZ, UK. s.curry@imperial.ac.uk
Roqué-Rosell
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Sweeney
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Zunszain
P A
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Leatherbarrow
R J
RJ
D000086042:3C Viral Proteases; D000818:Animals; D000998:Antiviral Agents / Q000494:pharmacology; D017124:Conserved Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology; D015195:Drug Design; D005536:Foot-and-Mouth Disease / Q000188:drug therapy / Q000201:enzymology / Q000821:virology; D029544:Foot-and-Mouth Disease Virus / Q000187:drug effects / Q000201:enzymology / Q000235:genetics / Q000472:pathogenicity; D008958:Models, Molecular; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D000998:Antiviral Agents; D015853:Cysteine Proteinase Inhibitors; D014764:Viral Proteins; D003546:Cysteine Endopeptidases; D000086042:3C Viral Proteases