Fig. 3 | Scientific Reports

Fig. 3

From: Cysteine protease I29 propeptide from Calotropis procera R. Br. As a potent cathepsin L inhibitor and its suppressive activity in breast cancer metastasis

Fig. 3

Inhibitory characteristics of SnuCalCpI15 against CTSL. (a) Structural models of SnuCalCp15 and SnuCalCpI15. The segment corresponding to SnuCalCpI15 (I29 domain) is colored following the pLDDT score (range: 0–100). The catalytic diad at the active site cleft and propeptide binding loop (PBL) are shown in yellow and magenta, respectively. (b, c) Flexible docking analysis of SnuCalCpI15 using CTSL (b) and closed CTSB (c) as receptors. The mature enzyme and its zymogen are superimposed. The C1A domain, its native propeptide, and SnuCalCpI15 are shown in gray, green, and cyan, respectively. The occluding loop of CTSB is represented as red, blue, and dark green for closed CTSB (propeptide-free), proCTSB, and CTSB–SnuCalCpI15 complex, respectively. (d) Alignment of C-terminal residues of SnuCalCpI15 at the CTSL active site cleft. (e) Docking of substrate Z-Phe-Arg-AMC with CTSL (Vina score: −8.1).

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