1. Approximately 25 amino acids at the exposed VP2 N terminus are highly vulnerable to proteolysis.
Side view of a fivefold cylinder, shown as a cross section on the right, depicting two of the five β-ribbons that form the cylinder in mauve and blue stick format.
Elevated fivefold cylinders enclosing pores that penetrate to the interior and are surrounded by ~15-Å-deep circular depressions.
Cross section of the channel, with specific residues at the base shown in space-filling format; residues G28-G-S-G-G-G-G-S-G-G-G-G-V40 from one VP2 are depicted in the pore, with glycines in white and serines in gray.
Elevations at the threefold axes that mediate surface protein and glycan receptor interactions in many parvoviruses.
Glycan-binding depressions surrounding the twofold axis that mediate viral tissue tropism by an unknown mechanism.
Elevations at the threefold axes that mediate surface protein and glycan receptor interactions in many parvoviruses.
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