Structure Elucidation of Coxsackievirus A16 in Complex with GPP3 Informs a Systematic Review of Highly Potent Capsid Binders to Enteroviruses - Fig 1

<p><b>(A)</b> CVA16 particle with capsid protein subunits VP1 (blue), VP2 (green), VP3 (red), VP4 (yellow) in surface representation. Inset in (<b>A</b>) 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>(B)</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.