7b2t
Crystal structure of Iripin-5 serpin from Ixodes ricinusCrystal structure of Iripin-5 serpin from Ixodes ricinus
Structural highlights
Publication Abstract from PubMedIripin-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. See AlsoReferences
|
|