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Journal Articles Archives of Biochemistry and Biophysics Year : 2019

Binding induced folding: Lessons from the kinetics of interaction between NTAIL and XD

Abstract

Intrinsically Disordered Proteins (IDPs) are a class of protein that exert their function despite lacking a well-defined three-dimensional structure, which is sometimes achieved only upon binding to their natural ligands. This feature implies the folding of IDPs to be generally coupled with a binding event, representing an interesting challenge for kinetic studies. In this review, we recapitulate some of the most important findings of IDPs binding-induced folding mechanisms obtained by analyzing their binding kinetics. Furthermore, by focusing on the interaction between the Measles virus NTAIL protein, a prototypical IDP, and its physiological partner, the X domain, we recapitulate the major theoretical and experimental approaches that were used to describe binding induced folding.
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hal-02341649 , version 1 (31-10-2019)

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Angelo Toto, Francesca Troilo, Lorenzo Visconti, Francesca Malagrinò, Christophe Bignon, et al.. Binding induced folding: Lessons from the kinetics of interaction between NTAIL and XD. Archives of Biochemistry and Biophysics, 2019, 671, pp.255-261. ⟨10.1016/j.abb.2019.07.011⟩. ⟨hal-02341649⟩
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