New structural insights into the inhibition of serine proteases by cyclic peptides from bacteria.
- 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 and 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.
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