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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.

DOI:10.1016/j.str.2020.10.006
PMID:33176159
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8184262/
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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引用本文的文献

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Fold-switching proteins.折叠转换蛋白
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Nat Commun. 2025 Jul 1;16(1):5622. doi: 10.1038/s41467-025-60759-5.
3
AlphaFold2's training set powers its predictions of some fold-switched conformations.AlphaFold2的训练集为其对一些折叠转换构象的预测提供了支持。

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。
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2
An alternative interpretation of the slow KaiB-KaiC binding of the cyanobacterial clock proteins.蓝藻生物钟蛋白的 KaiB-KaiC 缓慢结合的另一种解释。
Sci Rep. 2020 Jun 26;10(1):10439. doi: 10.1038/s41598-020-67298-7.
3
Cryo-EM structure and inhibitor design of human IAPP (amylin) fibrils.人胰淀素(胰岛淀粉样多肽)纤维的冷冻电镜结构和抑制剂设计。
Protein Sci. 2025 Apr;34(4):e70105. doi: 10.1002/pro.70105.
4
Evolving concepts of the protein universe.蛋白质世界的不断演变的概念。
iScience. 2025 Feb 13;28(3):112012. doi: 10.1016/j.isci.2025.112012. eCollection 2025 Mar 21.
5
Temperature-dependent fold-switching mechanism of the circadian clock protein KaiB.生物钟蛋白KaiB的温度依赖性折叠转换机制
Proc Natl Acad Sci U S A. 2024 Dec 17;121(51):e2412327121. doi: 10.1073/pnas.2412327121. Epub 2024 Dec 13.
6
Proteomic Evidence for Amyloidogenic Cross-Seeding in Fibrinaloid Microclots.纤维蛋白原样微栓中淀粉样蛋白形成的蛋白组学证据
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Elife. 2024 Oct 2;13:RP98665. doi: 10.7554/eLife.98665.
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AlphaFold2 Predicts Alternative Conformation Populations in Green Fluorescent Protein Variants.AlphaFold2 预测绿色荧光蛋白变体中的构象变化群体。
J Chem Inf Model. 2024 Sep 23;64(18):7135-7140. doi: 10.1021/acs.jcim.4c01388. Epub 2024 Sep 3.
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J Mol Evol. 2024 Dec;92(6):669-684. doi: 10.1007/s00239-024-10196-7. Epub 2024 Aug 30.
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Computational design of closely related proteins that adopt two well-defined but structurally divergent folds.紧密相关的蛋白质的计算设计,这些蛋白质采用两种定义明确但结构上不同的折叠。
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