Structural and biochemical characterization of the novel serpin Iripin-5 from Ixodes ricinus

0554123 - BC 2022 RIV GB eng J - Journal Article
Kaščáková, B. - Kotál, Jan - Martins, Larissa Almeida - Beránková, Z. - Langhansová, H. - Calvo, E. - Crossley, J. - Havlíčková, P. - Dyčka, F. - Prudníková, T. - Kutý, M. - Kotsyfakis, Michalis - Chmelař, J. - Smatanová, I.
Structural and biochemical characterization of the novel serpin Iripin-5 from Ixodes ricinus.
Acta Crystallographica Section D-Structural Biology. Roč. 77, SEP 1 2021 (2021), s. 1183-1196. ISSN 2059-7983. E-ISSN 2059-7983
Institutional support: RVO:60077344
Keywords : tick salivary protein * molecular simulations * crystal-structure * inhibitors * mechanism * crystallography * interface * ovalbumin * immunity * features * serpins * serine protease inhibitors * Iripin-5 * X-ray structure * Ixodes ricinus * tick saliva
OECD category: Biochemistry and molecular biology
Impact factor: 5.699, year: 2021
Method of publishing: Limited access
https://scripts.iucr.org/cgi-bin/paper?S2059798321007920

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.
Permanent Link: http://hdl.handle.net/11104/0328758