Selective inhibition of trypsins by insect peptides: role of P6-P10 loop
Kellenberger, C., Ferrat, G., Leone, P., Darbon, H., Roussel, A.(2003) Biochemistry 42: 13605-13612
- PubMed: 14622007
- DOI: https://doi.org/10.1021/bi035318t
- Primary Citation of Related Structures:
1WO9 - PubMed Abstract:
PMP-D2 and HI, two peptides from Locusta migratoria, were shown to belong to the family of tight-binding protease inhibitors. However, they interact weakly with bovine trypsin (K(i) around 100 nM) despite a trypsin-specific Arg at the primary specificity site P1. Here we demonstrate that they are potent inhibitors of midgut trypsins isolated from the same insect and of a fungal trypsin from Fusarium oxysporum (K(i)
Organizational Affiliation:
Centre d'Immunologie de Marseille-Luminy, UMR 145, Parc Scientifique et Technologique de Luminy, Case 906, 13009 Marseille, France. kellenberger@ciml.univ-mrs.fr