title: Crystallization and preliminary crystallographic studies of the copper-binding domain of the amyloid precursor protein of Alzheimer's disease.
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.
authors.affiliation: Biota Structural Biology Laboratory, St Vincent's Institute, Fitzroy, Victoria 3065, Australia.
authors.forename: Geoffrey K-W
authors.initials: GK
authors.lastname: Kong
authors.forename: Denise
authors.initials: D
authors.lastname: Galatis
authors.forename: Kevin J
authors.initials: KJ
authors.lastname: Barnham
authors.forename: Galina
authors.initials: G
authors.lastname: Polekhina
authors.forename: Julian J
authors.initials: JJ
authors.lastname: Adams
authors.forename: Colin L
authors.initials: CL
authors.lastname: Masters
authors.forename: Roberto
authors.initials: R
authors.lastname: Cappai
authors.forename: Michael W
authors.initials: MW
authors.lastname: Parker
authors.forename: William J
authors.initials: WJ
authors.lastname: McKinstry
mesh_terms: 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
chemical_list: D016564:Amyloid beta-Protein Precursor; D017931:DNA Primers; D003300:Copper