Skip to main content
. Author manuscript; available in PMC: 2023 Jul 24.
Published in final edited form as: Org Biomol Chem. 2022 Mar 9;20(10):2075–2080. doi: 10.1039/d1ob02127c

Fig. 1.

Fig. 1

Overlay of the interface regions of natural trypsin inhibitors showing similarities in the trypsin-binding segment, ie the highly conserved PPI interface. (a) Momordica charantia trypsin inhibitor A (MCTI-A, green, PDB ID 1F2S) is overlaid on six other trypsin inhibitors. (b) Enlarged view of the overlay with side chains of the P1, P1’, P2’ residues are highlighted as sticks.