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ABSTRACT: Background
Coagulation factor XII is a serine protease that is important for kinin generation and blood coagulation, cleaving the substrates plasma kallikrein and FXI.Objective
To investigate FXII zymogen activation and substrate recognition by determining the crystal structure of the FXII protease domain.Methods and results
A series of recombinant FXII protease constructs were characterized by measurement of cleavage of chromogenic peptide and plasma kallikrein protein substrates. This revealed that the FXII protease construct spanning the light chain has unexpectedly weak proteolytic activity compared to β-FXIIa, which has an additional nine amino acid remnant of the heavy chain present. Consistent with these data, the crystal structure of the light chain protease
SUBMITTER: Pathak M
PROVIDER: S-EPMC4418343 | biostudies-literature | 2015 Apr
REPOSITORIES: biostudies-literature