FIG 5.

Two protomers of the CVB3 capsid showing VP1 (blue), VP2 (green), and VP3 (red). VP4 lies on the inner capsid surface and is not shown. Pocket factor is shown (orange spheres) within the hydrophobic pocket of VP1. The mutation (Leu to Val) in CVB3/28 L1092V is shown as spheres (side chain carbons are light gray) in VP1 adjacent to the pocket factor. The side chain of leucine at VP1 residue 92 extends into the pocket and clashes with the pocket factor, and there is evidence that side chains extending into the pocket limit the length of pocket factor alkyl chains (49). Valine at residue 92 does not conflict with the longer pocket factor. The mutation (Ala to Thr) in CVB3/28 A3180T is shown as spheres in VP3 at a protomer-protomer interface with VP1 (near Pro1146, which is adjacent to the CAR contact residue Pro1145) (17). Both mutations were identified in a population derived from CVB3/28 after selection for survival at 37°C (27). The structure is from 1COV and rendered in PyMOL (50).