A tick protein with a modified Kunitz fold inhibits human tryptase.

Journal article

TdPI, a tick salivary gland product related to Kunitz/BPTI proteins is a potent inhibitor of human beta-tryptase. Kinetic assays suggest that three of the four catalytic sites of tryptase are blocked by TdPI, and that the inhibition of one of these involves a peptide flanking the Kunitz head. In the course of the inhibition, tryptase cleaves TdPI at several positions. Crystal structures of the TdPI head, on its own and in complex with trypsin, reveal features that are not found in classical K...

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Authors: Paesen, G; Siebold, C; Harlos, K; Peacey, M; Nuttall, P

• Publication status: Published
• Journal: Journal of molecular biology
• Volume: 368
• Issue: 4
• Pages: 1172-1186
• Publication date: 2007-05-01
• DOI: 10.1016/j.jmb.2007.03.011
• EISSN: 1089-8638
• ISSN: 0022-2836
• Language: English
• Keywords: Female; Humans; Models, Molecular; Mice, Inbred BALB C; Amino Acid Sequence; Mutation; Aprotinin; Cytoplasmic Granules; Skin; Mice; Male; Molecular Sequence Data; Ticks; Catalytic Domain; Tryptases; Mast Cells; Crystallography, X-Ray; Cytosol; Serine Proteinase Inhibitors; Protein Conformation; Animals