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. 2016 Jul 11;113(32):8997–9002. doi: 10.1073/pnas.1606595113

Fig. 3.

Fig. 3.

RV-C15a has a collapsed VP1 hydrophobic pocket. RV-A16 (A) and RV-C15a (B) are colored by polypeptides: VP1 (blue), VP2 (green), and VP3 (red). The volume of the VP1 hydrophobic pocket, calculated using PyMOL, is colored gold. (C) Residues lining the VP1 pocket of RV-C15a clash with pleconaril (a capsid-binding inhibitor against many EV but not RV-C) when superimposing the structures of RV-C15a and RV-B14 complexed with pleconaril. The VP1 GH loop (yellow) of RV-B14 is shown as Cα backbones, which adopts a conformation that can accommodate pleconaril. Red dashed lines indicate a distance of closer than 2.5 Å between a given atom of a RV-C15 residue (green) and a given atom of pleconaril (yellow). Oxygen, nitrogen, and sulfur atoms are colored red, dark blue, and dark yellow, respectively.