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Abstract
Thimet Oligopeptidase is a neuropeptidase in the M3 family of zinc metallopeptidases. It is responsible for the degradation of many bioactive peptides. Its most well‐known substrate is neurotensin, which is active both in the central nervous system and the periphery, but TOP also cleaves a number of other small peptides. The most intriguing characteristic of TOP is its "fuzzy" substrate recognition that allows it to cleave oligopeptides with no obvious sequence similarity while maintaining a high degree of specificity for those sites. By crystallizing TOP in the presence of substrates we have found a unique binding site that interacts with the C‐terminal end of peptide substrates. We are currently investigating the energetics of peptide binding by calorimetry.
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