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Crystallization and preliminary crystallographic studies of the copper-binding domain of the amyloid precursor protein of Alzheimer's disease.
- Source :
- Acta Crystallographica: Section F (Wiley-Blackwell); Jan2005, Vol. 61 Issue 1, p93-95, 3p
- Publication Year :
- 2005
-
Abstract
- 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<superscript>2+</superscript> 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. [ABSTRACT FROM AUTHOR]
- Subjects :
- CRYSTALLIZATION
CHEMICAL bonds
COPPER
AMYLOID
GLYCOPROTEINS
ALZHEIMER'S disease
Subjects
Details
- Language :
- English
- ISSN :
- 17443091
- Volume :
- 61
- Issue :
- 1
- Database :
- Complementary Index
- Journal :
- Acta Crystallographica: Section F (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 18502649
- Full Text :
- https://doi.org/10.1107/S1744309104029744