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![[Figure 4]](ql5001fig4mag.jpg)
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Figure 4
WIN compounds inhibit VP1 receptor binding. (a) Structure of the human rhinovirus HRV14 capsid in complex with the antiviral compound WIN 52084 comprising the coat protein VP1 (green), VP2 (cyan), VP3 (magenta) and VP4 (yellow). A pocket factor, most likely a fatty acid, bound within a hydrophobic pocket of VP1 inspired the synthesis of the WIN compounds. The blue circle highlights a VP1 pentamer, shown in a close-up view (below) bound with WIN 52084 (orange, chemical structure shown above; PDB entry 1rud; Hadfield et al., 1995  ). (b) Schematic showing receptor binding to a cleft in the VP1 pentamer in the absence of a bound WIN compound or pocket factor. Below: WIN compounds bind tightly to the pocket and induce a conformation that is incompatible with receptor binding to VP1. (c) Zoom into the hydrophobic pocket of human rhinovirus HRV16 VP1 occupied by WIN 65099 (orange and mesh, chemical structure shown below; PDB entry 1qjy; Hadfield et al., 1999). |
![[Figure 4]](ql5001fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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