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首页> 外文期刊>Journal of Molecular Biology >The common architecture of cross-beta amyloid.
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The common architecture of cross-beta amyloid.

机译：跨β淀粉样蛋白的常见结构。

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Amyloid fibril deposition is central to the pathology of more than 30 unrelated diseases including Alzheimer's disease and Type 2 diabetes. It is generally accepted that amyloid fibrils share common structural features despite each disease being characterised by the deposition of an unrelated protein or peptide. The structure of amyloid fibrils has been studied using X-ray fibre diffraction and crystallography, solid-state NMR and electron paramagnetic resonance, and many different, sometimes opposing, models have been suggested. Many of these models are based on the original interpretation of the cross-beta diffraction pattern for cross-beta silk in which beta-strands run perpendicular to the fibre axis, although alternative models include beta-helices and natively structured proteins. Here, we have analysed opposing model structures and examined the necessary structural elements within the amyloid core structure, as well as producing idealised models to test the limits of the core conformation. Our work supports the view that amyloid fibrils share a number of common structural features, resulting in characteristic diffraction patterns. This pattern may be satisfied by structures in which the strands align close to perpendicular to the fibre axis and are regularly arranged to form beta-sheet ribbons. Furthermore, the fibril structure contains several beta-sheets that associate via side-chain packing to form the final protofilament structure.
机译：淀粉样蛋白原纤维沉积对于包括阿尔茨海默氏病和2型糖尿病在内的30多种无关疾病的病理至关重要。尽管每种疾病都以不相关的蛋白质或肽沉积为特征，但淀粉样蛋白原纤维具有共同的结构特征，这是公认的。已经使用X射线纤维衍射和晶体学，固态NMR和电子顺磁共振研究了淀粉样蛋白原纤维的结构，并且已经提出了许多不同的，有时是相反的模型。这些模型中的许多模型都是基于对交叉β丝的交叉β衍射图样的原始解释，其中β链垂直于纤维轴延伸，尽管其他模型包括β螺旋和天然结构化蛋白质。在这里，我们分析了相反的模型结构，并检查了淀粉样蛋白核心结构内的必要结构元素，并生成了理想化的模型来测试核心构象的极限。我们的工作支持这样的观点，即淀粉样蛋白原纤维具有许多共同的结构特征，从而导致特征衍射图样。该图案可以通过以下结构来满足，在该结构中，股线接近于垂直于纤维轴线的方向对准并且规则地布置以形成β片状带。此外，原纤维结构包含几个β-折叠，它们通过侧链堆积结合形成最终的原丝结构。

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