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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt 1):93-5. Epub 2004 Dec 2.

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

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1
Biota Structural Biology Laboratory, St Vincent's Institute, Fitzroy, Victoria 3065, Australia.

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.

PMID:
16508101
PMCID:
PMC1952382
DOI:
10.1107/S1744309104029744
[Indexed for MEDLINE]
Free PMC Article
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