离子转运蛋白的研究是蛋白质科学领域的研究热点。目前在镁离子转运机理的研究上，相对于镁离子的生物体内丰度和重要性，我们对其转运机理和意义严重缺乏认知。镁离子通道蛋白CorA不能单独外溢镁离子，而另一镁离子通道蛋白MgtE可以。镁离子转运蛋白CorC含有一个MgtE胞质区具有的CBS结构域，可以协助CorA实现镁离子外溢。我们拟鉴定CorC以及其CBS结构域与腺苷类配体的结合特性，测定CorC与配体以及金属离子等复合物的晶体结构，阐释其在配体调控下的构象变化以及配体调控下的蛋白-蛋白相互作用，研究CorC受配体调控参与CorA镁离子转运系统行使离子转运功能的分子机理，探索CorA与MgtE镁离子转运系统离子转运特性的异同。同时我们将以CorC的CBS结构域研究为基础，探索人类CBS结构域蛋白质的CBS结构域突变引起人类遗传性疾病的分子机理，为此类遗传性疾病的发生、发展和干预提供理论基础指导。

Considering the biological abundance and importance of Mg2+, there is a surprising lack of information regarding the proteins that transport Mg2+, the mechanisms by which they do so, and their physiological roles within the cell. The magnesium channel CorA could not efflux Mg2+ independently whereas another magnesium channel MgtE does. A magnesium transporter CorC could assist CorA to efflux Mg2+, containing a CBS domain pair which is also observed in the cytosolic domain of MgtE. In this study, we would identify the profile of adenine nucleotide ligand and so on CorC binds, determine the crystal structures of CorC-ligands and CorC-ion complex, reveal the protein conformational change induced by ligands, discover the interaction between CorC and other proteins involving in ligand binding, illustrate the mechanism of CorC involved in CorA magnesium transporter system, and then study the difference of CorA and MgtE magnesium transporter system. On the other side, point or deletion mutations in CBS domains of several human enzymes and membrane channels are associated with hereditary diseases, including homocystinuria, retinitis pigmentosa, Bartter syndrome, osteopetrosis, Dent disease, Wolff-Parkinson-White syndrome, and familial hypertrophic cardiomyopathy. Based on the mechanism of CorC involved in magnesium transporter and sensing adenine nucleotides, we would study the mechanisms how mutations in CBS domains leads to losing the abilities of binding ligands or proteins and how mutations are involved in human diseases.