A twisted four-sheeted model for an amyloid fibril.
A twisted four-sheeted model for an amyloid fibril.
复制标题
淀粉样原纤维的扭曲四片模型。
DOI：
10.1016/j.str.2005.06.010
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发表时间：
2005
期刊：
影响因子：
--
通讯作者：
Regan,Lynne
中科院分区：
文献类型：
--
作者：
Wang,Jimin;Gulich,Susanne;Bradford,Catharine;Ramirez-Alvarado,Marina;Regan,Lynne
The formation of amyloid fibers and their deposition in the body is a characteristic of a number of devastating human diseases. Here, we propose a structural model, based on X-ray diffraction data, for the basic structure of an amyloid fibril formed by using the variants of the B1 domain of IgG binding protein G ofStreptococcus. The model for the fibril incorporates four β sheets in a bundle with a diameter of 45 Å. Its cross-section, or layer, consists of four strands, one strand from each sheet. Layers stack on top of each other to form the fibril, which has an overall helical twist with a periodicity of about 154 Å. Each strand interacts in a parallel fashion with the strands in the layers above and below it, in an infinite β sheet. Some geometric features of this model and the logic behind it may be applicable for constructing other related cross-β amyloid fibrils.
