Crystallization and preliminary crystallographic studies of the copper-binding domain of the amyloid precursor protein of Alzheimer's disease

Alzheimer ' s disease is thought to be triggered by production of the amyloid beta (A beta) peptide through proteolytic cleavage of the amyloid precursor protein (APP). The binding of Cu2+ to the copper-binding domain (CuBD) of APP reduces the production of A beta in cell-culture and animal studies. It is expected that structural studies of the CuBD will lead to a better understanding of how copper binding causes A beta depletion and will define a potential drug target. The crystallization of CuBD in two different forms suitable for structure determination is reported here.