| Literature DB >> 32696383 |
Ke Yang1, Munehito Arai2, Peter E Wright3.
Abstract
The unique structural flexibility of intrinsically disordered proteins (IDPs) is central to their diverse functions in cellular processes. Protein-protein interactions involving IDPs are frequently transient and dynamic in nature. Nuclear magnetic resonance (NMR) spectroscopy is an especially powerful tool for characterizing the structural propensities, dynamics, and interactions of IDPs. Here we describe applications of the Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion experiment in combination with NMR titrations to characterize the kinetics and mechanisms of interactions between intrinsically disordered proteins and their targets. We illustrate the method with reference to interactions between the activation domain of the human T-cell leukemia virus type-I (HTLV-1) basic leucine zipper protein (HBZ) and its cellular binding partner, the KIX domain of the transcriptional coactivator CBP.Entities:
Keywords: CPMG; IDP; Protein dynamics; Protein interaction; Relaxation dispersion
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Year: 2020 PMID： 32696383 PMCID： PMC7605514 DOI： 10.1007/978-1-0716-0524-0_34
Source DB: PubMed Journal: Methods Mol Biol ISSN： 1064-3745