Structural Studies of Herpesvirus Proteases

Structural studies of herpesvirus proteases establish that they belong to a new class of serine proteases and contain a novel Ser-His-His catalytic triad. Peptidomimetic inhibitors bind to the protease by forming an anti-parallel beeta-sheet with the enzyme. There are large conformational changes in the protease upon inhibitor binding, indicating that the protease is an induced-fit enzyme. Further studies are needed to understand the molecular basis for the dimerization requirement of the protease.