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

Geoffrey K-W Kong, Denise Galatis, Kevin Jeffrey Barnham, Galina Polekhina, Julian J Adams, Colin Louis Masters, Roberto Cappai, Michael William Parker, William J McKinstry

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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.
Original languageEnglish
Pages (from-to)93 - 95
Number of pages3
JournalActa Crystallographica Section F: Structural Biology Communications
Issue number1
Publication statusPublished - 2005

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