Protein surface charge of trypsinogen changes its activation pattern.

ABSTRACT:

Background

Trypsinogen is the inactive precursor of trypsin, a serine protease that cleaves proteins and peptides after arginine and lysine residues. In this study, human trypsinogen was used as a model protein to study the influence of electrostatic forces on protein-protein interactions. Trypsinogen is active only after its eight-amino-acid-long activation peptide has been cleaved off by another protease, enteropeptidase. Trypsinogen can also be autoactivated without the involvement of enteropeptidase. This autoactivation process can occur if a trypsinogen molecule is activated by another trypsin molecule and therefore is based on a protein-protein interaction.

Results

Based on a rational protein design based on autoactivation-defective guinea pig trypsinogen, several amin

SUBMITTER: Buettner K 

PROVIDER: S-EPMC4299543 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature