Malagrinò Francesca, Diop Awa, Pagano Livia, Nardella Caterina, Toto Angelo, Gianni Stefano
Istituto Pasteur, Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche "A. Rossi Fanelli" and Istituto di Biologia e Patologia Molecolari Del CNR, Sapienza Università, di Roma, 00185, Rome, Italy.
Istituto Pasteur, Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche "A. Rossi Fanelli" and Istituto di Biologia e Patologia Molecolari Del CNR, Sapienza Università, di Roma, 00185, Rome, Italy.
Curr Opin Struct Biol. 2022 Feb;72:153-160. doi: 10.1016/j.sbi.2021.11.004. Epub 2021 Dec 11.
Intrinsically disordered proteins (IDPs) can be generally described as a class of proteins that lack a well-defined ordered structure in isolation at physiological conditions. Upon binding to their physiological ligands, IDPs typically undergo a disorder-to-order transition, which may or may not lead to the complete folding of the IDP. In this short review, we focus on some of the key findings pertaining to the mechanisms of such induced folding. In particular, first we describe the general features of the reaction; then, we discuss some of the most remarkable findings obtained from applying protein engineering in synergy with kinetic studies to induced folding; and finally, we offer a critical view on some of the emerging themes when considering the structural heterogeneity of IDPs vis-à-vis to their inherent frustration.
内在无序蛋白（IDP）通常可被描述为一类在生理条件下单独存在时缺乏明确有序结构的蛋白质。在与它们的生理配体结合后，IDP通常会经历从无序到有序的转变，这可能会也可能不会导致IDP的完全折叠。在这篇简短的综述中，我们聚焦于一些与这种诱导折叠机制相关的关键发现。具体而言，首先我们描述该反应的一般特征；然后，我们讨论通过将蛋白质工程与动力学研究协同应用于诱导折叠所获得的一些最显著的发现；最后，当考虑IDP的结构异质性及其内在的受挫情况时，我们对一些新兴主题提出批判性观点。
