Unraveling the Thermodynamics of Ultra-tight Binding of Intrinsically Disordered Proteins.

ABSTRACT: Protein interactions mediated by the intrinsically disordered proteins (IDPs) are generally associated with lower affinities compared to those between globular proteins. Here, we characterize the association between the intrinsically disordered HigA2 antitoxin and its globular target HigB2 toxin from Vibrio cholerae using competition ITC experiments. We demonstrate that this interaction reaches one of the highest affinities reported for IDP-target systems (K _D = 3 pM) and can be entirely attributed to a short, 20-residue-long interaction motif that folds into α-helix upon binding. We perform an experimentally based decomposition of the IDP-target association parameters into folding and binding contributions, which allows a direct comparison of the binding contribut

SUBMITTER: Zavrtanik U 

PROVIDER: S-EPMC8438204 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature