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. 2015 Oct 20;11(10):e1005165. doi: 10.1371/journal.ppat.1005165

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© 2015 De Colibus et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Fig 1 — (A) CVA16 particle with capsid protein subunits VP1 (blue), VP2 (green), VP3 (red), VP4 (yellow) in surface representation. Inset in (A) shows the location of CVA16 inhibitor binding in the pocket (shown schematically in blue) lying below the canyon floor, here occupied by a natural pocket factor (magenta, in sticks representation). The VP1 subunits at the icosahedral five-fold axis are shown as a blue surface overlaid on a cartoon representation whereas the other subunits are in light gray. A segment around the five-fold axis is cut away to reveal two pockets. (B) A selection of 3-(4-pyridyl)-2-imidazolidinone derivative structures. The following chemical moieties are labeled in GPP3: A, pyridine ring; B, imidazole moiety; C, phenoxy group.