New Structural Insights into the Inhibition of Serine Proteases by Cyclic Peptides from Bacteria Review Article

The inhibition of enzymes employing a nucleophilic serine residue by natural products has been studied for many years. More recently, high-resolution structural analyses have begun to augment kinetic analyses. In this issue of Chemistry & Biology, Schulz and colleagues describe the crystal structure of scyptolin A, a cyclic peptide produced by cyanobacteria, complexed with elastase. Together with structures for a related inhibitor bound to trypsin, the work may assist in the design of reversible serine protease inhibitors.