Use of EPR power saturation to analyze the membrane-docking geometries of peripheral proteins: applications to C2 domains.

Nathan J Malmberg, Joseph J Falke
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引用次数: 65

Abstract

Despite the central importance of peripheral membrane proteins to cellular signaling and metabolic pathways, the structures of protein-membrane interfaces remain largely inaccessible to high-resolution structural methods. In recent years a number of laboratories have contributed to the development of an electron paramagnetic resonance (EPR) power saturation approach that utilizes site-directed spin labeling to determine the key geometric parameters of membrane-docked proteins, including their penetration depths and angular orientations relative to the membrane surface. Representative applications to Ca(2+)-activated, membrane-docking C2 domains are described.

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使用EPR功率饱和分析外周蛋白的膜对接几何形状:在C2结构域的应用。
尽管外周膜蛋白对细胞信号传导和代谢途径至关重要,但高分辨率结构方法在很大程度上仍无法获得蛋白质-膜界面的结构。近年来,许多实验室致力于电子顺磁共振(EPR)功率饱和方法的发展,该方法利用定点自旋标记来确定膜停靠蛋白的关键几何参数,包括它们的渗透深度和相对于膜表面的角取向。描述了Ca(2+)活化的膜对接C2结构域的代表性应用。
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