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 structu...
| Автори: | , |
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| Формат: | Journal article |
| Мова: | English |
| Опубліковано: |
2003
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| Резюме: | 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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