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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 5.

Figure 5

(A) Inhibitory cyclic peptides bound to the surface of a serine protease. The cyclic peptide SFTI (magenta, 1SFI.pdb) inhibits trypsin in a canonical manner, upain (orange, 2NWN.pdb) binds to the prime side of uPA, and the fVIIa inhibitors E-76 (green, 1DVA.pdb) and A-183 (blue, 1JBU.pdb) bind to protease exosites. (B) Antibodies provide an alternative scaffold on which to build protease inhibitors with a high degree of specificity. The antibody E2 (magenta) binds in the protease active site (MT-SP1, 3BN9.pdb) in a non-canonical manner, while the Fab40 (orange, 3K2U.pdb) antibody inhibits HGFA while binding outside the protease active site through an allosteric mechanism.