Iripin-5 is the main Ixodes ricinus salivary serpin, which acts as a modulator of host defence mechanisms by impairing neutrophil migration, suppressing nitric oxide production by macrophages and altering complement functions. Iripin-5 influences host immunity and shows high expression in the salivary glands. Here, the crystal structure of Iripin-5 in the most thermodynamically stable state of serpins is described. In the reactive-centre loop, the main substrate-recognition site of Iripin-5 is likely to be represented by Arg342, which implies the targeting of trypsin-like proteases. Furthermore, a computational structural analysis of selected Iripin-5-protease complexes together with interface analysis revealed the most probable residues of Iripin-5 involved in complex formation.

Department of Chemistry Faculty of Science University of South Bohemia in Ceske Budejovice 370 05 Ceske Budejovice Czech Republic

Department of Medical Biology Faculty of Science University of South Bohemia in Ceske Budejovice 370 05 Ceske Budejovice Czech Republic

Institute of Parasitology Biology Centre of the Czech Academy of Sciences 370 05 Ceske Budejovice Czech Republic

Laboratory of Malaria and Vector Research National Institute of Allergy and Infectious Diseases National Institutes of Health Rockville MD 20852 USA

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