Pacifastin-related peptides: structural and functional characteristics of a family of serine peptidase inhibitors |
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Authors: | Breugelmans Bert Simonet Gert van Hoef Vincent Van Soest Sofie Vanden Broeck Jozef |
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Affiliation: | Department of Animal Physiology, Zoological Institute K.U. Leuven, Naamsestraat 59, B-3000 Leuven, Belgium. Bert.Breugelmans@bio.kuleuven.be |
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Abstract: | Members of the pacifastin family are serine peptidase inhibitors, found in arthropods and have many members within different insect orders. Based on their structural characteristics, inhibitors of this peptide family are divided into two groups (I and II). Members of both groups exhibit specificity towards different types of serine peptidases. In addition, group I inhibitors display species selectivity. The specificity and selectivity of these inhibitors depends on the nature of their P1 residue and on additional interaction sites at the inhibitor's surface. Functional analysis studies have shown that crustacean pacifastin plays a key role in the immune response, whereas insect pacifastin-like peptides have multiple regulatory functions in processes involved in immunity, reproduction, phase transition, etc. |
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