Open AccessCrystallization and preliminary crystallographic studies of the copper‐binding domain of the amyloid precursor protein of Alzheimer's disease
Author(s) -
Kong Geoffrey K.W.,
Galatis Denise,
Barnham Kevin J.,
Polekhina Galina,
Adams Julian J.,
Masters Colin L.,
Cappai Roberto,
Parker Michael W.,
McKinstry William J.
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309104029744
Subject(s) - crystallization , amyloid precursor protein , p3 peptide , copper , cleavage (geology) , peptide , amyloid (mycology) , disease , chemistry , alzheimer's disease , biochemistry of alzheimer's disease , biophysics , biochemistry , crystallography , microbiology and biotechnology , biology , medicine , pathology , inorganic chemistry , paleontology , organic chemistry , fracture (geology)
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 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.