Fig. 5.

Backbone model of the structure of five symmetry-related VP2 (shown in different colors) belonging to different trimers around the capsid pore at one of the capsid five-fold axes (center region). Mutated residues at the intertrimer interfaces are represented as space-filling models (except Ile-167, which is shown as a ball-and-stick model). The residues whose side chains were found to be involved in a heat-induced conformational change and externalization of the VP2 N termini are shown in yellow. The residues whose side chains could be truncated without abolishing the conformational rearrangement are shown in violet.