Corbalan-Garcia Senena, Gómez-Fernández Juan C
Departamento de Bioquímica y Biología Molecular-A, Facultad de Veterinaria, Regional Campus of International Excellence "Campus Mare Nostrum", Universidad de Murcia, 30100 Murcia, Spain.
Biochim Biophys Acta. 2014 Jun;1838(6):1536-47. doi: 10.1016/j.bbamem.2014.01.008. Epub 2014 Jan 16.
C2 domains are membrane-binding modules that share a common overall fold: a single compact Greek-key motif organized as an eight-stranded anti-parallel β-sandwich consisting of a pair of four-stranded β-sheets. A myriad of studies have demonstrated that in spite of sharing the common structural β-sandwich core, slight variations in the residues located in the interconnecting loops confer C2 domains with functional abilities to respond to different Ca(2+) concentrations and lipids, and to signal through protein-protein interactions as well. This review summarizes the main structural and functional findings on Ca(2+) and lipid interactions by C2 domains, including the discovery of the phosphoinositide-binding site located in the β3-β4 strands. The wide variety of functions, together with the different Ca(2+) and lipid affinities of these domains, converts this superfamily into a crucial player in many functions in the cell and more to be discovered. This Article is Part of a Special Issue Entitled: Membrane Structure and Function: Relevance in the Cell's Physiology, Pathology and Therapy.
C2结构域是膜结合模块，具有共同的整体折叠结构：一个单一紧凑的希腊钥匙基序，由一对四链β折叠片层组成的八链反平行β三明治结构。大量研究表明，尽管共享共同的结构β三明治核心，但位于连接环中的残基的微小变化赋予C2结构域对不同Ca(2+)浓度和脂质做出反应的功能能力，以及通过蛋白质-蛋白质相互作用进行信号传导的能力。本综述总结了关于C2结构域与Ca(2+)和脂质相互作用的主要结构和功能研究结果，包括位于β3-β4链中的磷酸肌醇结合位点的发现。这些结构域的多种功能以及不同的Ca(2+)和脂质亲和力，使其成为细胞中许多功能的关键参与者，还有更多有待发现。本文是名为：膜结构与功能：在细胞生理、病理和治疗中的相关性的特刊的一部分。
