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. 1998 Feb;72(2):1210–1218. doi: 10.1128/jvi.72.2.1210-1218.1998

FIG. 6.

FIG. 6

Computer representation of HRV16 showing that two of the three drug dependence mutations are exposed on the virion surface. The protein shell contains 60 subunits (protomers) organized as 12 pentamers. (A) For clarity, only one pentamer is shown (in stereo projection). Both mutated residues are shown in red (V1210A and M1103T). The green patches in the canyon region identify the foot print for the cellular receptor ICAM-1 (36). One promoter is highlighted (gray) to show that both residues are located at a protomer-protomer interface. (B) Protomer-protomer interface showing how residue V1210 within the gray protomer contacts residue Y3183 within its neighboring protomer (yellow). (C) Stereo projection of a protomer-protomer interface showing how residue M1103 within one protomer (gray) makes contact with residue Q1161 within a neighboring protomer (yellow). In panels B and C, the surfaces of the contacting residues are depicted as meshes. (Crystallographic coordinates were provided by M. G. Rossmann. Projections were made by using the computer program GRASP.)

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