What makes functional amyloids work?

What makes functional amyloids work?
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DOI:
10.1080/10409238.2022.2113030
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发表时间:
2022-08
影响因子:
6.5
通讯作者:
--
中科院分区:
生物学2区
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--
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虽然首次描述的背景下,疾病,交叉β(淀粉样蛋白)原纤维也被发现作为功能实体在所有王国的生活。然而,交叉β原纤维基序的具体特性是什么,这些特性传达了生物学功能,使它们特别适合其特定目的,并将它们与生物学中发现的其他原纤维区分开来?本文通过论证交叉β纤维是高度周期性的、稳定的和自模板化的结构,其形成伴随着大量的构象变化,导致其核心和框架序列的多聚化来解决这些问题。对这些特性中的每一个的讨论之后是功能性交叉β原纤维的选定实例,其显示通常如何通过利用这些特性中的许多特性来实现功能。
Although first described in the context of disease, cross-β (amyloid) fibrils have also been found as functional entities in all kingdoms of life. However, what are the specific properties of the cross-β fibril motif that convey biological function, make them especially suited for their particular purpose, and distinguish them from other fibrils found in biology? This review approaches these questions by arguing that cross-β fibrils are highly periodic, stable, and self-templating structures whose formation is accompanied by substantial conformational change that leads to a multimerization of their core and framing sequences. A discussion of each of these properties is followed by selected examples of functional cross-β fibrils that show how function is usually achieved by leveraging many of these properties.
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