Abstract
The members of the Pacifastin family are serine protease inhibitors found in insects and crustacean. They are either small inhibitors (made of one consensus cysteine-rich motif) or proteins (4-9 motifs). Some of these inhibitors are characterized by a species selectivity for the trypsin inhibition. Structural data discriminate the small inhibitors that apparently look very similar into two groups. Interestingly, the inhibitors that display species selectivity fall in the same structural group.
Keywords: pacifastin, protease inhibitor, insect, structure, species selectivity
Protein & Peptide Letters
Title: Structure-Activity Relationship Within the Serine Protease Inhibitors of the Pacifastin Family
Volume: 12 Issue: 5
Author(s): Christine Kellenberger and Alain Roussel
Affiliation:
Keywords: pacifastin, protease inhibitor, insect, structure, species selectivity
Abstract: The members of the Pacifastin family are serine protease inhibitors found in insects and crustacean. They are either small inhibitors (made of one consensus cysteine-rich motif) or proteins (4-9 motifs). Some of these inhibitors are characterized by a species selectivity for the trypsin inhibition. Structural data discriminate the small inhibitors that apparently look very similar into two groups. Interestingly, the inhibitors that display species selectivity fall in the same structural group.
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Cite this article as:
Kellenberger Christine and Roussel Alain, Structure-Activity Relationship Within the Serine Protease Inhibitors of the Pacifastin Family, Protein & Peptide Letters 2005; 12 (5) . https://dx.doi.org/10.2174/0929866054395239
DOI https://dx.doi.org/10.2174/0929866054395239 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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