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Structural and biochemical characterization of the novel serpin Iripin-5 from Ixodes ricinus
Acta Crystallographica Section D ( IF 2.2 ) Pub Date : 2021-09-02 , DOI: 10.1107/s2059798321007920
Barbora Kascakova 1 , Jan Kotal 2 , Larissa Almeida Martins 3 , Zuzana Berankova 2 , Helena Langhansova 2 , Eric Calvo 4 , Joel A Crossley 1 , Petra Havlickova 1 , Filip Dycka 1 , Tatyana Prudnikova 1 , Michal Kuty 1 , Michail Kotsyfakis 2 , Jindrich Chmelar 2 , Ivana Kuta Smatanova 1
Affiliation  

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.

中文翻译:

蓖麻硬蜱新型丝氨酸蛋白酶抑制剂 Iripin-5 的结构和生化特征

Iripin-5 是蓖麻硬蜱唾液中的主要丝氨酸蛋白酶抑制剂,它通过损害中性粒细胞迁移、抑制巨噬细胞产生一氧化氮和改变补体功能来充当宿主防御机制的调节剂。Iripin-5 影响宿主免疫力并在唾液腺中高表达。在此,描述了丝氨酸蛋白酶抑制剂热力学最稳定状态下的 Iripin-5 的晶体结构。在反应中心环中,Iripin-5 的主要底物识别位点可能由 Arg342 代表,这意味着胰蛋白酶样蛋白酶的靶向。此外,对选定的 Iripin-5-蛋白酶复合物进行计算结构分析以及界面分析揭示了 Iripin-5 最有可能参与复合物形成的残基。
更新日期:2021-09-02
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