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

Clicks: 217
ID: 13070
2019
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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 N 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.
Reference Key
toto2019bindingarchives Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Toto, Angelo;Troilo, Francesca;Visconti, Lorenzo;Malagrinò, Francesca;Bignon, Christophe;Longhi, Sonia;Gianni, Stefano;
Journal archives of biochemistry and biophysics
Year 2019
DOI
S0003-9861(19)30409-6
URL
Keywords Keywords not found

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