Nuclear Magnetic Resonance Approaches for Characterizing Protein-Protein Interactions
Nuclear Magnetic Resonance Approaches for Characterizing Protein-Protein Interactions
复制标题
用于表征蛋白质-蛋白质相互作用的核磁共振方法
DOI：
10.1007/978-1-4939-7362-0_10
复制
发表时间：
2017
期刊：
影响因子：
--
通讯作者：
Shimada Ichio
中科院分区：
文献类型：
--
作者：
Toyama Yuki;Mase Yoko;Kano Hanaho;Yokogawa Mariko;Osawa Masanori;Shimada Ichio
钾离子(K+)通道的门控受各种蛋白质-蛋白质相互作用(PPI)调节。这些PPI的结构研究不仅为理解K+通道的门控机制提供了有用的信息，也为开发针对K+通道的药物化合物提供了有用的信息。在这里，我们描述了一种被称为交叉饱和(CS)的核磁共振波谱方法，它可以准确地确定蛋白质复合体的结合表面，并应用于研究G蛋白偶联内向整流K+通道和G蛋白α亚基之间的相互作用。
The gating of potassium ion (K+) channels is regulated by various kinds of protein-protein interactions (PPIs). Structural investigations of these PPIs provide useful information not only for understanding the gating mechanisms of K+channels, but also for developing the pharmaceutical compounds targeting K+channels. Here, we describe a nuclear magnetic resonance spectroscopic method, termed the cross saturation (CS) method, to accurately determine the binding surfaces of protein complexes, and its application to the investigation of the interaction between a G protein-coupled inwardly rectifying K+channel and a G protein α subunit.