Key result
Crystallographic analysis of the poliovirus empty capsid at 2.9 Å resolution revealed disordered N-terminal extensions and a displaced VP0 scissile bond compared to mature virions.
The 2.9 Å resolution structure of the poliovirus empty capsid provides insights into the initiation of encapsidation and the RNA-dependent autocatalytic cleavage of VP0.
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Structural insights into poliovirus assembly add no clinical guidance; extends models of capsid maturation for future mechanistic studies.
Basavappa et al. (1994) studied Poliovirus. Crystallographic analysis of the poliovirus empty capsid at 2.9 Å resolution revealed disordered N-terminal extensions and a displaced VP0 scissile bond compared to mature virions.
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