期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 61, 期 -, 页码 93-95出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309104029744
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Alzheimer ' s disease is thought to be triggered by production of the amyloid beta (A beta) 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 A beta 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 A beta depletion and will define a potential drug target. The crystallization of CuBD in two different forms suitable for structure determination is reported here.
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