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. Author manuscript; available in PMC: 2014 Sep 1.
Published in final edited form as: Chembiochem. 2010 Nov 22;11(17):2341–2346. doi: 10.1002/cbic.201000442

Figure 2.

Figure 2

Competitive, active site inhibitors of proteases. (A) Inhibitors bind in the active site, but not in a substrate-like manner. Peptide extensions bind in specificity subsites, and can interact with the catalytic residues (rectangle). Crystal structures of (B) a serine protease (matriptase/MT-SP1, 1EAW.pdb) in complex with the standard mechanism inhibitor aprotinin, and (C) the cystatin stefin A in complex with a cysteine protease (cathepsin H, 1NB5.pdb). The portion of stefin A that interacts with the protease is colored in green. Both inhibitors bind in the active site groove of their targets.