Fig. 1: The zymogen activation motif of TTSPs are cleaved by trypsin-like serine proteases and their residue composition is distinct to each TTSP. | Nature Communications

Fig. 1: The zymogen activation motif of TTSPs are cleaved by trypsin-like serine proteases and their residue composition is distinct to each TTSP.

From: Structural basis of TMPRSS11D specificity and autocleavage activation

Fig. 1: The zymogen activation motif of TTSPs are cleaved by trypsin-like serine proteases and their residue composition is distinct to each TTSP.

a Schematic of an inactive (zymogen) TTSP at the cell surface. The catalytic Serine Protease (SP) domain is connected to the non-catalytic (stem) domains through a disulfide bond (S-S) and the zymogen activation motif peptide bond, shown as a pink line. The zymogen motif peptide bond is cleaved (indicated with scissors) to form (b) the matured TTSP that has enzymatic activity and can cleave protein and/or peptide substrates. c Multiple sequence alignment of the zymogen activation motif of all human TTSPs. TTSPs are colored by TTSP subfamily; hepsin/TMPRSS-black; HAT/DESC-blue; matriptase-magenta; corin-orange. The length of the zymogen activation motif is indicated in parentheses for each TTSP. Scissors and a dashed black line indicate where TTSPs are cleaved during protease zymogen activation.

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