Opening of the two-fold channels in the 80S empty capsid.

<p>Contacts between pentamers along the two-fold and three-fold axes in the 80S empty particle (A) as compared to those present in the native HRV2 capsid (B). The capsid proteins VP1 (blue), VP2 (green) and VP3 (red) are depicted as ribbons. The position of the symmetry axes is indicated in (B). (C) Close-up view of the channel formed at the two-fold axes in the 80S particle, seen from the interior of the capsid. The VP2 and VP3 subunits surrounding the channel are represented as cartoons and the side chains of VP2 exposed at the interface are depicted as sticks. The lines crossing the cavity correspond to distances of 10.2 Å (a) and 30.5 Å (b). (D) Charge distribution on the walls of the channel at the two-fold axes. In order to show the surface of the longitudinal walls, a side view of the channel (perpendicular to the direction of the symmetry axis) has been slabbed. The surface is represented with the electrostatic potential, colored in blue and red for positive and negative charges, respectively. The relevant residues are shown as sticks and labeled. The direction of the two-fold symmetry axis is also indicated with a line and a black symbol.