Molecular recognition of proteins regulating transport of copper ions in cells

为了揭示调控铜离子在细胞内运输的分子机制，我注意到了铜伴侣CCS和需要铜的酶SOD1之间的特定相互作用。在细胞内，铜结合形式的CCS特异性识别apo SOD1，然后将铜离子输送到SOD1。CCS由三个结构域组成，其中一个中央结构域(CCS-DII)起着识别SOD1的作用。在这项研究中，我用重组的CCS-DII和SOD1蛋白进行了体外生化试验，发现了这两种蛋白相互结合的要求。

To reveal a molecular mechanism regulating the intracellular transport of copper ions, I have noted specific interactions between a copper chaperone, CCS, and a copper-requiring enzyme, SOD1. Inside cells, a copper-bound form of CCS specifically recognizes apo SOD1 and then delivers a copper ion to SOD1. CCS consists of three domains, among which a central domain(CCS-dII) plays a role in recognizing SOD1. In this study, I have performed in vitro biochemical tests using recombinant CCS-dII and SOD1 proteins and found the requirements for these two proteins to associate with each other.