Download MendeleyImplications for viral uncoating from the structure of bovine enterovirus.
Smyth, M., Tate, J., Hoey, E., Lyons, C., Martin, S., Stuart, D.(1995) Nat Struct Biol 2: 224-231
- PubMed: 7773791
- DOI: https://doi.org/10.1038/nsb0395-224
- Primary Citation of Related Structures:
1BEV - PubMed 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.
Organizational Affiliation:
Laboratory of Molecular Biophysics, Oxford, UK.
