title: Implications for viral uncoating from the structure of bovine enterovirus.
abstract: We have determined the crystal structure of a bovine enterovirus, revealing that the topologies of the major capsid proteins and the overall architecture of the virion are similar to those of related picornaviruses. The external loops joining beta-strands are truncated and the canyon region is partially filled by an extension of the VP3 G-H loop giving the viral capsid a relatively smooth appearance. These changes may have implications for cell attachment. In spite of these differences the virus maintains a hydrophobic pocket within VP1, occupied by a specific 'pocket factor' which appears to be myristic acid. These observations support the proposal that a kinetic equilibrium exists between occupied and unoccupied pocket states, with occupation inhibiting uncoating.
authors.affiliation: Laboratory of Molecular Biophysics, Oxford, UK.
authors.forename: M
authors.initials: M
authors.lastname: Smyth
authors.forename: J
authors.initials: J
authors.lastname: Tate
authors.forename: E
authors.initials: E
authors.lastname: Hoey
authors.forename: C
authors.initials: C
authors.lastname: Lyons
authors.forename: S
authors.initials: S
authors.lastname: Martin
authors.forename: D
authors.initials: D
authors.lastname: Stuart
mesh_terms: D000818:Animals; D002213:Capsid / Q000737:chemistry*; D036022:Capsid Proteins; D002417:Cattle; D003460:Crystallization; D004770:Enterovirus / Q000737:chemistry*; D008958:Models, Molecular; D015394:Molecular Structure; D010849:Picornaviridae / Q000737:chemistry; D011487:Protein Conformation
chemical_list: D036022:Capsid Proteins