Binding induced folding: Lessons from the kinetics of interaction between NTAIL and XD.
Arch Biochem Biophys
; 671: 255-261, 2019 08 15.
Article
em En
| MEDLINE
| ID: mdl-31326517
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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Base de dados:
MEDLINE
Assunto principal:
Proteínas Virais
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Dobramento de Proteína
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Proteínas Intrinsicamente Desordenadas
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Vírus do Sarampo
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article