[HTML][HTML] Serine and cysteine proteases are translocated to similar extents upon formation of covalent complexes with serpins: Fluorescence perturbation and …
R Swanson, MP Raghavendra, W Zhang… - Journal of Biological …, 2007 - ASBMB
CrmA is a" cross-class" serpin family inhibitor of the proapoptotic serine protease, granzyme
B, as well as cysteine proteases of the caspase family. To determine whether crmA inhibits
these structurally diverse proteases by a common conformational trapping mechanism, we
mapped the position of the protease in crmA complexes with granzyme B or caspase-1 by
fluorescence perturbation and fluorescence resonance energy transfer (FRET) analyses of
site-specific fluorophore-labeled crmAs. A reactive loop P6 NBD label underwent similar …
B, as well as cysteine proteases of the caspase family. To determine whether crmA inhibits
these structurally diverse proteases by a common conformational trapping mechanism, we
mapped the position of the protease in crmA complexes with granzyme B or caspase-1 by
fluorescence perturbation and fluorescence resonance energy transfer (FRET) analyses of
site-specific fluorophore-labeled crmAs. A reactive loop P6 NBD label underwent similar …