阿尔茨海默病淀粉样前体蛋白铜结合结构域的结晶及初步晶体学研究
Crystallization and preliminary crystallographic studies of the copper-binding domain of the amyloid precursor protein of Alzheimer's disease.
作者信息
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
机构信息
Biota Structural Biology Laboratory, St Vincent's Institute, Fitzroy, Victoria 3065, Australia.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt 1):93-5. doi: 10.1107/S1744309104029744. Epub 2004 Dec 2.
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.
摘要
阿尔茨海默病被认为是由淀粉样前体蛋白（APP）经蛋白水解切割产生β淀粉样蛋白（Aβ）肽所引发的。在细胞培养和动物研究中，Cu2+与APP的铜结合结构域（CuBD）结合可减少Aβ的产生。预计对CuBD的结构研究将有助于更好地理解铜结合如何导致Aβ减少，并确定一个潜在的药物靶点。本文报道了适合结构测定的两种不同形式的CuBD的晶体化情况。
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