Crystallization and preliminary crystallographic studies of the copper-binding domain of the amyloid precursor protein of Alzheimer's disease.
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.
Kong
Geoffrey K-W
GK
Biota Structural Biology Laboratory, St Vincent's Institute, Fitzroy, Victoria 3065, Australia.
Galatis
Denise
D
Barnham
Kevin J
KJ
Polekhina
Galina
G
Adams
Julian J
JJ
Masters
Colin L
CL
Cappai
Roberto
R
Parker
Michael W
MW
McKinstry
William J
WJ
D000544:Alzheimer Disease / Q000378:metabolism*; D016564:Amyloid beta-Protein Precursor / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D003300:Copper / Q000378:metabolism*; D003460:Crystallization; D017931:DNA Primers; D006801:Humans; D010843:Pichia; D011487:Protein Conformation; D014961:X-Ray Diffraction
D016564:Amyloid beta-Protein Precursor; D017931:DNA Primers; D003300:Copper