In recent years our understanding of amyloid structure has been revolutionised by innovations in cryo-electron microscopy, electron diffraction and solid-state NMR. These techniques have yielded high-resolution structures of fibrils isolated from patients with neurodegenerative disease, as well as those formed from amyloidogenic proteins in vitro. The results not only show the expected cross-β amyloid structure, but also reveal that the amyloid fold is unexpectedly diverse and complex. Here, we discuss this diversity, highlighting dynamic regions, ligand binding motifs, cavities, non-protein components, and structural polymorphism. Collectively, these variations combine to allow the generic amyloid fold to be realised in three dimensions in different ways, and this diversity may be related to the roles of fibrils in disease.

中文翻译：

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淀粉样蛋白结构：不仅仅是交叉β折叠。

近年来，冷冻电子显微镜、电子衍射和固态核磁共振的创新彻底改变了我们对淀粉样蛋白结构的理解。这些技术已经产生了从神经退行性疾病患者中分离出的原纤维的高分辨率结构，以及在体外由淀粉样蛋白形成的原纤维的结构。结果不仅显示了预期的交叉β淀粉样蛋白结构，而且还揭示了淀粉样蛋白折叠出乎意料的多样化和复杂性。在这里，我们讨论这种多样性，重点介绍动态区域、配体结合基序、空腔、非蛋白质成分和结构多态性。总的来说，这些变异结合起来使得通用淀粉样蛋白折叠能够以不同的方式在三个维度上实现，并且这种多样性可能与原纤维在疾病中的作用有关。