Structural highlights
Publication Abstract from PubMed
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.
Structural and biochemical characterization of the novel serpin Iripin-5 from Ixodes ricinus.,Kascakova B, Kotal J, Martins LA, Berankova Z, Langhansova H, Calvo E, Crossley JA, Havlickova P, Dycka F, Prudnikova T, Kuty M, Kotsyfakis M, Chmelar J, Kuta Smatanova I Acta Crystallogr D Struct Biol. 2021 Sep 1;77(Pt 9):1183-1196. doi: , 10.1107/S2059798321007920. Epub 2021 Aug 23. PMID:34473088[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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References
- ↑ Kascakova B, Kotal J, Martins LA, Berankova Z, Langhansova H, Calvo E, Crossley JA, Havlickova P, Dycka F, Prudnikova T, Kuty M, Kotsyfakis M, Chmelar J, Kuta Smatanova I. Structural and biochemical characterization of the novel serpin Iripin-5 from Ixodes ricinus. Acta Crystallogr D Struct Biol. 2021 Sep 1;77(Pt 9):1183-1196. PMID:34473088 doi:10.1107/S2059798321007920