7B2T
Crystal structure of Iripin-5 serpin from Ixodes ricinus
This is a non-PDB format compatible entry.
Summary for 7B2T
| Entry DOI | 10.2210/pdb7b2t/pdb |
| Descriptor | Serpin-4 precursor, putative, MAGNESIUM ION, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | serpin, inhibitor, hydrolase inhibitor, ixodes ricinus, hydrolase |
| Biological source | Ixodes scapularis (Black-legged tick) More |
| Total number of polymer chains | 4 |
| Total formula weight | 83286.01 |
| Authors | Kascakova, B.,Kuta Smatanova, I. (deposition date: 2020-11-27, release date: 2021-10-06, Last modification date: 2024-01-31) |
| Primary citation | Kascakova, B.,Kotal, J.,Martins, L.A.,Berankova, Z.,Langhansova, H.,Calvo, E.,Crossley, J.A.,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, 77:1183-1196, 2021 Cited by PubMed Abstract: 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. PubMed: 34473088DOI: 10.1107/S2059798321007920 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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