Structural and biochemical characterization of the novel serpin Iripin-5 from Ixodes ricinus
| Autor: | Joel A. Crossley, Tatyana Prudnikova, Larissa Almeida Martins, Helena Langhansová, Zuzana Beránková, Filip Dycka, Michal Kuty, Jindrich Chmelar, Petra Havlickova, Barbora Kascakova, Jan Kotál, Eric Calvo, Michail Kotsyfakis, Ivana Kuta Smatanova |
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| Rok vydání: | 2021 |
| Předmět: |
Proteases
Erythrocytes Ixodes ricinus Neutrophils Complex formation Anti-Inflammatory Agents Serpin Nitric oxide Mice chemistry.chemical_compound Structural Biology Animals Enzyme Inhibitors Cells Cultured Serpins Stable state Ixodes biology Chemistry Macrophages Host defence biology.organism_classification Research Papers Cell biology Mice Inbred C57BL Rabbits Interface analysis |
| Zdroj: | Acta Crystallogr D Struct Biol |
| ISSN: | 2059-7983 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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