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折叠开关蛋白的功能和调节作用。

Functional and Regulatory Roles of Fold-Switching Proteins.

机构信息

National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA; National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.

National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA; National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.

出版信息

Structure. 2021 Jan 7;29(1):6-14. doi: 10.1016/j.str.2020.10.006. Epub 2020 Nov 10.

Abstract

Fold-switching proteins respond to cellular stimuli by remodeling their secondary structures and changing their functions. Whereas several previous reviews have focused on various structural, physical-chemical, and evolutionary aspects of this newly emerging class of proteins, this minireview focuses on how fold switching modulates protein function and regulates biological processes. It first compares and contrasts fold switchers with other known types of proteins. Second, it presents examples of how various proteins can change their functions through fold switching. Third, it demonstrates that fold switchers can regulate biological processes by discussing two proteins, RfaH and KaiB, whose dramatic secondary structure remodeling events directly affect gene expression and a circadian clock, respectively. Finally, this minireview discusses how the field of protein fold switching might advance.

摘要

构象转换蛋白通过重塑其二级结构并改变其功能来响应细胞刺激。虽然之前的几篇综述已经关注了这一新兴蛋白质类别的各种结构、物理化学和进化方面,但本篇小综述重点关注构象转换如何调节蛋白质功能并调节生物过程。它首先比较和对比了构象转换蛋白与其他已知类型的蛋白质。其次,它展示了各种蛋白质如何通过构象转换来改变其功能。第三,它通过讨论两个蛋白质 RfaH 和 KaiB,说明了构象转换蛋白如何通过调节生物过程,它们的剧烈二级结构重塑事件分别直接影响基因表达和生物钟。最后,这篇小综述讨论了蛋白质构象转换领域可能的进展。

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本文引用的文献

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Exploring the sequence fitness landscape of a bridge between protein folds.探索蛋白质折叠之间桥的序列适应性景观。
PLoS Comput Biol. 2020 Oct 13;16(10):e1008285. doi: 10.1371/journal.pcbi.1008285. eCollection 2020 Oct.
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Orchestration of Circadian Timing by Macromolecular Protein Assemblies.大分子蛋白质组装对生物钟的调控。
J Mol Biol. 2020 May 29;432(12):3426-3448. doi: 10.1016/j.jmb.2019.12.046. Epub 2020 Jan 13.

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