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变构调节蛋白酶体核心颗粒与调节颗粒之间的相互作用。

Allostery Modulates Interactions between Proteasome Core Particles and Regulatory Particles.

作者信息

Coffino Philip, Cheng Yifan

机构信息

Laboratory of Cellular Biophysics, Department of Molecular and Cell Biology, Rockefeller University, New York, NY 10065, USA.

Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, CA 94158, USA.

出版信息

Biomolecules. 2022 May 30;12(6):764. doi: 10.3390/biom12060764.

DOI:10.3390/biom12060764
PMID:35740889
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9221237/
Abstract

Allostery-regulation at distant sites is a key concept in biology. The proteasome exhibits multiple forms of allosteric regulation. This regulatory communication can span a distance exceeding 100 Ångstroms and can modulate interactions between the two major proteasome modules: its core particle and regulatory complexes. Allostery can further influence the assembly of the core particle with regulatory particles. In this focused review, known and postulated interactions between these proteasome modules are described. Allostery may explain how cells build and maintain diverse populations of proteasome assemblies and can provide opportunities for therapeutic interventions.

摘要

远处位点的变构调节是生物学中的一个关键概念。蛋白酶体表现出多种形式的变构调节。这种调节通讯的距离可超过100埃,并且可以调节蛋白酶体两个主要模块之间的相互作用:其核心颗粒和调节复合物。变构还可以进一步影响核心颗粒与调节颗粒的组装。在这篇重点综述中,描述了这些蛋白酶体模块之间已知的和推测的相互作用。变构可能解释细胞如何构建和维持蛋白酶体组装的多样化群体,并可为治疗干预提供机会。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed23/9221237/d4b28e4071a1/biomolecules-12-00764-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed23/9221237/d4b28e4071a1/biomolecules-12-00764-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ed23/9221237/d4b28e4071a1/biomolecules-12-00764-g001.jpg

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本文引用的文献

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2
Mapping the energetic and allosteric landscapes of protein binding domains.绘制蛋白质结合域的能量和别构景观。
Nature. 2022 Apr;604(7904):175-183. doi: 10.1038/s41586-022-04586-4. Epub 2022 Apr 6.
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Localized Proteasomal Degradation: From the Nucleus to Cell Periphery.局部化的蛋白酶体降解:从细胞核到细胞外周。
细胞中 26S 蛋白酶体监测方法揭示了 PSMA3 C 端在 26S 完整性中的关键作用。
Biomolecules. 2023 Jun 15;13(6):992. doi: 10.3390/biom13060992.
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From Deep Mutational Mapping of Allosteric Protein Landscapes to Deep Learning of Allostery and Hidden Allosteric Sites: Zooming in on "Allosteric Intersection" of Biochemical and Big Data Approaches.从变构蛋白构象的深度突变映射到变构和隐藏变构位点的深度学习:聚焦于生化和大数据方法的“变构交集”。
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