Figure 20.

Proposed mechanism of dimer disruption and allosteric inhibition of herpesvirus proteases. Inhibitor binding in the core of the protein precludes folding of the C-terminal helices, preventing both dimerization and proper formation of the oxyanion holes formed by two conserved arginines. The catalytic serine is unperturbed, but the substrate binding site may be occluded. Reprinted from ref (176). Copyright 2014 American Chemical Society.