X RAY CRYSTALLOGRAPHIC STUDIES--COPPER CHAPERONE LYS7

超氧化物歧化酶催化超氧化物歧化为过氧化氢和氧气。这种酶的活性要求每个亚基有一个双金属铜、锌中心。在酵母中，只有在铜伴侣蛋白Lys7存在的情况下，铜才能插入到超氧化物歧化酶(SOD1)中。这个方案的目的是解决Lys7的三维结构，包括金属离子的存在和不存在，以及Lys7与SOD1的络合。在人类中，SOD1与家族性肌萎缩侧索硬化症(Lou Gehrig病)有关，对铜插入机制的详细了解应有助于开发这种疾病的新疗法。

Superoxide dismutase catalyzes the disproportionation of superoxide to hydrogen peroxide and dioxygen. For activity, this exzyme requires one dimetallic Cu,Zn center per subunit. In yeast, the insertion of the copper into superoxide dismutase (Sod1) only occurs in the presence of the copper chaperone protein Lys7. The objective of this proposal is to solve the three dimensional structures of Lys7, with and without the metal ions, and Lys7 complexed with Sod1. In humans, Sod1 has been linked to familial amyotrophic lateral sclerosis (Lou Gehrig's Disease), and a detailed understanding of the mechanism of copper insertion should lead to the development of new therapies for this disease.