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

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Geoffrey K-W KongWilliam J McKinstry

Abstract

Alzheimer's disease is thought to be triggered by production of the amyloid beta (Abeta) 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 Abeta 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 Abeta depletion and will define a potential drug target. The crystallization of CuBD in two different forms suitable for structure determination is reported here.

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Citations

Jun 12, 2012·The Journal of Biological Chemistry·Loredana SpoerriRoberto Cappai
Oct 29, 2009·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Ya Hui HungRobert Alan Cherny

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