High-resolution crystal structure of the catalytic domain of human dual-specificity phosphatase 26

This study presents crystal structures of the catalytic domain of human DUSP26 and a catalytically inactive mutant at 1.67 and 2.20 Å resolution, respectively.

Structural asymmetry of procaspase-7 bound to a specific inhibitor

The first structural analysis of a procaspase-7 variant bound to a specific inhibitor, Ac-DEVD-CHO, revealed a structural asymmetry that the two L2 loops in homodimeric procaspase-7 served as inherent L2 and L2' loops forming a complete active site in one monomer, which may be responsible to a basal activity level, but not in the other. This provides insight into the basal activity of procaspase-7 and the folding mechanism during caspase-7 activation.

Structural basis for the dephosphorylating activity of PTPRQ towards phosphatidylinositide substrates

The crystal structure of human PTPRQ and the following kinetic data provide the explanation for its dephosphosphorylating activity towards phosphatidyl inositides.