title: Foot-and-mouth disease virus 3C protease: recent structural and functional insights into an antiviral target.
abstract: The 3C protease from foot-and-mouth disease virus (FMDV 3C(pro)) is critical for viral pathogenesis, having vital roles in both the processing of the polyprotein precursor and RNA replication. Although recent structural and functional studies have revealed new insights into the mechanism and function of the enzyme, key questions remain that must be addressed before the potential of FMDV 3C(pro) as an antiviral drug target can be realised.
authors.affiliation: Biophysics Section, Division of Cell and Molecular Biology, Blackett Laboratory, Imperial College, Exhibition Road, London SW7 2AZ, UK. s.curry@imperial.ac.uk
authors.forename: Stephen
authors.initials: S
authors.lastname: Curry
authors.forename: Núria
authors.initials: N
authors.lastname: Roqué-Rosell
authors.forename: Patricia A
authors.initials: PA
authors.lastname: Zunszain
authors.forename: Robin J
authors.initials: RJ
authors.lastname: Leatherbarrow
mesh_terms: D000086042:3C Viral Proteases; D000818:Animals; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000378:metabolism; D005536:Foot-and-Mouth Disease / Q000188:drug therapy / Q000201:enzymology; D029544:Foot-and-Mouth Disease Virus / Q000201:enzymology* / Q000472:pathogenicity; D011498:Protein Precursors / Q000378:metabolism; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012313:RNA / Q000096:biosynthesis; D012367:RNA, Viral / Q000096:biosynthesis; D014764:Viral Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D014779:Virus Replication / Q000502:physiology
chemical_list: D011498:Protein Precursors; D012367:RNA, Viral; D014764:Viral Proteins; D012313:RNA; D003546:Cysteine Endopeptidases; D000086042:3C Viral Proteases