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从免疫原性肽到内在无序蛋白质

From Immunogenic Peptides to Intrinsically Disordered Proteins.

作者信息

Dyson H Jane, Wright Peter E

机构信息

Department of Integrative Structural and Computational Biology, Scripps Research, 10550 North Torrey Pines Road, La Jolla, CA 92037.

出版信息

Isr J Chem. 2023 Oct;63(10-11). doi: 10.1002/ijch.202300051. Epub 2023 May 11.

DOI:10.1002/ijch.202300051
PMID:38454968
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10919381/
Abstract

It is hard to evaluate the role of individual mentors in the genesis of important ideas. In the case of our realization that proteins do not have to be stably folded to be functional, the influence of Richard Lerner and our collaborative work in the 1980s on the conformations of immunogenic peptides provided a base level of thinking about the nature of polypeptides in water solutions that led us to formulate and develop our ideas on the importance of intrinsic disorder in proteins. This review describes how the insights gained into the behavior of peptides led directly to the realization that proteins were not only capable of being functional while disordered, but also that disorder provided a distinct functional advantage in many important cellular processes.

摘要

很难评估个别导师在重要思想起源中所起的作用。就我们认识到蛋白质不一定需要稳定折叠才具有功能而言，理查德·勒纳在20世纪80年代对免疫原性肽构象的影响以及我们的合作研究，为思考水溶液中多肽的性质提供了一个基础层面的思路，这促使我们形成并发展了关于蛋白质内在无序重要性的观点。这篇综述描述了对肽行为的深入了解如何直接导致我们认识到蛋白质不仅在无序状态下能够发挥功能，而且无序在许多重要的细胞过程中提供了独特的功能优势。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0d66/10919381/154cfbd9b972/nihms-1967382-f0007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0d66/10919381/b34827575952/nihms-1967382-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0d66/10919381/330ec88d6e11/nihms-1967382-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0d66/10919381/fd710911c383/nihms-1967382-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0d66/10919381/1ad218e08ffa/nihms-1967382-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0d66/10919381/52a9571189f8/nihms-1967382-f0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0d66/10919381/e9f230c0c674/nihms-1967382-f0006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0d66/10919381/154cfbd9b972/nihms-1967382-f0007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0d66/10919381/b34827575952/nihms-1967382-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0d66/10919381/330ec88d6e11/nihms-1967382-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0d66/10919381/fd710911c383/nihms-1967382-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0d66/10919381/1ad218e08ffa/nihms-1967382-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0d66/10919381/52a9571189f8/nihms-1967382-f0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0d66/10919381/e9f230c0c674/nihms-1967382-f0006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0d66/10919381/154cfbd9b972/nihms-1967382-f0007.jpg

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本文引用的文献

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Multivalency enables unidirectional switch-like competition between intrinsically disordered proteins.多价性使无规卷曲蛋白质之间的单向类开关竞争成为可能。
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Sortase-mediated segmental labeling: A method for segmental assignment of intrinsically disordered regions in proteins.Sortase 介导的分段标记：一种用于蛋白质中固有无序区域分段分配的方法。
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变构作用在促进解离过程中的分子基础。
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Polyelectrolyte interactions enable rapid association and dissociation in high-affinity disordered protein complexes.聚电解质相互作用使高亲和力无规蛋白复合物能够快速缔合和解离。
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Role of Backbone Dynamics in Modulating the Interactions of Disordered Ligands with the TAZ1 Domain of the CREB-Binding Protein.骨架动力学在调节无规配体与 CREB 结合蛋白 TAZ1 结构域相互作用中的作用。
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Long-range regulation of p53 DNA binding by its intrinsically disordered N-terminal transactivation domain.其无规则 N 端转录激活域对 p53 DNA 结合的远程调控。
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Facilitated dissociation of transcription factors from single DNA binding sites.促进转录因子从单个 DNA 结合位点解离。
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Hypersensitive termination of the hypoxic response by a disordered protein switch.由紊乱的蛋白质开关导致的缺氧反应超敏终止。
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How Does Your Protein Fold? Elucidating the Apomyoglobin Folding Pathway.蛋白质如何折叠？阐明去辅肌红蛋白的折叠途径。
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