The structural basis of specific protease-inhibitor interactions at the plant-pathogen interface
The structural basis of specific protease-inhibitor interactions at the plant-pathogen interface
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DOI：
10.1016/j.sbi.2013.07.013
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发表时间：
2013-12-01
影响因子：
6.8
通讯作者：
Van der Hoorn, Renier A. L.
中科院分区：
文献类型：
--
作者：
Hoerger, Anja C.;Van der Hoorn, Renier A. L.
宿主与病原体的拮抗相互作用为分子水平上的共同进化过程提供了有趣的见解。对模型植物番茄分泌的免疫蛋白酶及其与不同的不相关病原体衍生抑制剂的相互作用的研究表明，这些抑制剂对不同的宿主蛋白酶表现出显着的选择性，并且宿主蛋白酶在相互作用表面积累了干扰抑制剂结合的变异残基。在这里，我们总结和讨论了最近的发现，并使用结构模型来识别支撑蛋白酶选择性的分子特征。观察到的基本原理可以转化为分泌性免疫水解酶及其假定抑制剂的其他例子。
Antagonistic host-pathogen interactions offer intriguing insights into coevolutionary processes at the molecular level. Studies on secreted immune proteases from the model plant tomato and their interactions with different unrelated pathogen-derived inhibitors revealed that the inhibitors exhibit a remarkable selectivity towards different host proteases, and that the host proteases accumulate variant residues at the interaction surfaces that interfere with inhibitor binding. Here, we summarize and discuss the recent findings and use structural models to identify the molecular features underpinning protease selectivity. The observed basic principles translate to other examples of secreted immune hydrolases and their putative inhibitors.