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

Journal Article · Sat Jan 01 04:00:00 EST 2005 · Acta Crystallographica. Section F

DOI:https://doi.org/10.1107/S1744309104029744· OSTI ID:22356074

Kong, Geoffrey K.-W. ^[1]; Galatis, Denise; Barnham, Kevin J. ^[2]; Polekhina, Galina; Adams, Julian J. ^[1]; Masters, Colin L. ^[2]; Cappai, Roberto ^[2]; Parker, Michael W.

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1. Biota Structural Biology Laboratory, St Vincent’s Institute, 9 Princes Street, Fitzroy, Victoria 3065 (Australia)
2. Department of Pathology, The University of Melbourne, Victoria 3010 (Australia)

The binding of Cu{sup 2+} ions to the copper-binding domain of the amyloid precursor protein of Alzheimer’s disease reduces the production of the amyloid β peptide, which is centrally involved in Alzheimer’s disease. Structural studies of the copper-binding domain will provide a basis for structure-based drug design that might prove useful in treating this devastating disease. Alzheimer’s disease is thought to be triggered by production of the amyloid β (Aβ) peptide through proteolytic cleavage of the amyloid precursor protein (APP). The binding of Cu{sup 2+} to the copper-binding domain (CuBD) of APP reduces the production of Aβ 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 Aβ depletion and will define a potential drug target. The crystallization of CuBD in two different forms suitable for structure determination is reported here.

• OSTI ID: 22356074
• Journal Information: Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 1 Vol. 61; ISSN ACSFCL; ISSN 1744-3091
• Country of Publication: United Kingdom
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CLEAVAGE
COPPER
CRYSTALLIZATION
DESIGN
POTENTIALS
PRECURSOR