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Document Figure 1 Schematic illustration of the icosahedral rhinovirus 14. (a) Shown is the icosahedron comprised of 60 copies each of VP1 (light gray), VP2 (black), and VP3 (gray). The shaded circles around each five-fold axis indicate the canyon positions. Also indicated is the approximate position of the VP1 hydrophobic pocket that lies underneath the surface of the virion. (b) An icosahedral pentamer is expanded with one viral protomer shown as a protein ribbon diagram. (c) This pentamer is seen in a cutaway view. Here VP1 is white, VP2 and VP4 black, and VP3 gray. A capsid-binding compound is depicted as black spheres inside the VP1 ribbon diagram. The cross hatched regions on the (c) schematic (right) indicate areas that disorder when HRV14 crystals are exposed to acid. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_490.html (2 of 2) [4/9/2004 12:32:48 AM]
Document A. The Canyon Page 491 The HRVs have been divided into the major and minor receptor groups based on two identified cellular receptors [3]. The major group, which is comprised of approximately 90 serotypes, binds to the intercellular adhesion molecule 1 (ICAM-1) [20]. The minor group, about 10 serotypes, binds to the low density lipoprotein receptor family [21]. The canyons are depressions approximately 15 to 20 Å deep that encircle each icosahedral five-fold axis (Figure 1). When first seen in HRV 14, these canyons were postulated to be the site at which a cellular receptor would bind. Subsequent electron-microscopic data revealed that ICAM-1 does indeed bind in the canyon as predicted, although in a somewhat different orientation than early models [22,23]. These canyons allow the receptor binding sites to escape immunological surveillance because the canyons are too narrow to allow an immunoglobulin to contact the canyon floor. Directly underneath the floor of the canyon lies a second important structure, the VP1 hydrophobic pocket. B. The VP1 Hydrophobic Pocket The VP1 hydrophobic pocket is the site where the capsid-binding compounds reside. This hydrophobic pocket in VP1 was not initially apparent in the HRV14 structure because it exists in a closed conformation in the native HRV14. The addition of a capsid-binding antiviral agent induces the pocket to open. This was first seen by Smith and coworkers when the first crystal structure of a capsid-binding drug, WIN 51711, was solved bound in HRV14 [24]. (WIN is the designation for a Sterling Winthrop compound.) This was a seminal event in the structure-based design of these capsid-binding compounds; before this structure was solved the exact site at which the compounds bound was unknown. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_491.html [4/9/2004 12:33:24 AM]
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