Protein-Protein Recognition Control by Modulating Electrostatic Interactions
Protein-Protein Recognition Control by Modulating Electrostatic Interactions
复制标题
通过调节静电相互作用控制蛋白质-蛋白质识别
DOI：
10.1021/pr100027k
复制
发表时间：
2010-06-01
影响因子：
4.4
通讯作者：
Li, Wenxin
中科院分区：
文献类型：
--
作者：
Han, Song;Yin, Shijin;Li, Wenxin
蛋白质-蛋白质控制识别仍然是一个巨大的挑战，它的发展取决于理解这些相互作用发生的化学和生物学机制。在这里，我们描述了一种蛋白质-蛋白质控制识别技术的基础上发生的蛋白质之间的占主导地位的静电相互作用。我们设计了一个钾通道抑制剂BmP 05-T，与野生型BmP 05的同源性为90.32%。带负电荷的残基从非结合界面移位到BmP 05抑制剂的结合界面，使得BmP 05-T现在使用BmP 05非结合界面作为结合界面。这种开关表明，在蛋白质识别过程中，非结合界面能够控制蛋白质结合界面的方向。BmP 05-T肽的新功能发现表明，这里描述的控制识别技术具有在许多生物场景中设计和利用功能蛋白的潜力。
Protein-protein control recognition remains a huge challenge, and its development depends on understanding the chemical and biological mechanisms by which these interactions occur. Here we describe a protein-protein control recognition technique based on the dominant electrostatic interactions occurring between the proteins. We designed a potassium channel inhibitor, BmP05-T, that was 90.32% identical to wild-type BmP05. Negatively charged residues were translocated from the nonbinding interface to the binding interface of BmP05 inhibitor, such that BmP05-T now used BmP05 nonbinding interface as the binding interface. This switch demonstrated that nonbinding interfaces were able to control the orientation of protein binding interfaces in the process of protein protein recognition. The novel function findings of BmP05-T peptide suggested that the control recognition technique described here had the potential for use in designing and utilizing functional proteins in many biological scenarios.