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结构在无规则蛋白区域中的功能重要性。

The functional importance of structure in unstructured protein regions.

机构信息

Conway Institute of Biomolecular & Biomedical Research, University College Dublin, Belfield, Dublin 4, Ireland; Division of Cancer Biology, The Institute of Cancer Research, 237 Fulham Road, London SW3 6JB, UK.

出版信息

Curr Opin Struct Biol. 2019 Jun;56:155-163. doi: 10.1016/j.sbi.2019.03.009. Epub 2019 Apr 17.

DOI:10.1016/j.sbi.2019.03.009
PMID:31003202
Abstract

After two decades of research, intrinsically disordered regions (IDRs) are established as a widespread phenomenon. The growing understanding of the significant functional role of IDRs has challenged the structure-function paradigm, proving irrefutably that a stably folded structure is not a strict requirement for function. Nonetheless, (un)structure-function relationships remain at the core of IDR-mediated interactions. An IDR can populate a continuously transitioning continuum of structural conformations from fully disordered to stable globular states. In these ensembles, only subsets of conformations are binding competent, with intramolecular IDR contacts serving as important intermolecular binding determinants. Here, we review our current understanding of different types of intramolecular IDR interactions, their effects on IDR complex formation and their modes of biological regulation.

摘要

经过二十年的研究,无规区域(IDR)已被确定为一种广泛存在的现象。对 IDR 重要功能作用的认识不断加深,挑战了结构-功能范式,无可辩驳地证明了稳定折叠结构不是功能的严格要求。尽管如此,(无)结构-功能关系仍然是 IDR 介导相互作用的核心。IDR 可以从完全无序到稳定的球状状态,在连续过渡的结构构象连续体中存在。在这些集合中,只有构象的子集具有结合能力,分子内 IDR 接触作为重要的分子间结合决定因素。在这里,我们回顾了我们对不同类型的分子内 IDR 相互作用、它们对 IDR 复合物形成的影响以及它们的生物调节方式的现有理解。

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