Crystal Structures of the Viral Protease Npro Imply Distinct Roles for the Catalytic Water in Catalysis
Thomas Zögg, Michael Sponring, Sabrina Schindler, Maria Koll, Rainer Schneider, Hans Brandstetter, and Bernhard Auer

Abstract:
The bifunctional protein Npro is a key effector of pestiviruses, which are a major cause for lifestock disease and pathology. Using its proteolytic function, Npro liberates itself from the viral polyprotein. Free Npro then abolishes host cell antiviral defense mechanisms by suppression of IFN-α/β. The Npro crystal structures suggest the putative catalytic water to act in distinct ways along the proposed cleavage reaction. They offer a mechanism for its cis-cleaving activity and open opportunities to use Npro as pharmaceutical target.

The open access article can be found  here.

Reviewed by Peter Lackner