Identification and structural characterization of an intermediate in the folding of the measles virus X domain
Articolo
Data di Pubblicazione:
2016
Citazione:
Identification and structural characterization of an intermediate in the folding of the measles virus X domain / D. Bonetti, C. Camilloni, L. Visconti, S. Longhi, M. Brunori, M. Vendruscolo, S. Gianni. - In: THE JOURNAL OF BIOLOGICAL CHEMISTRY. - ISSN 0021-9258. - 291:20(2016), pp. 10886-10892. [10.1074/jbc.M116.721126]
Abstract:
Although most proteins fold by populating intermediates, the transient nature of such states makes it difficult to characterize their structures. In this work we identified and characterized the structure of an intermediate of the X domain of phosphoprotein (P) of measles virus. We obtained this result by a combination of equilibrium and kinetic measurements and NMR chemical shifts used as structural restraints in replica-averaged metadynamics simulations. The structure of the intermediate was then validated by rationally designing four mutational variants predicted to affect the stability of this state. These results provide a detailed view of an intermediate state and illustrate the opportunities offered by a synergistic use of experimental and computational methods to describe non-native states at atomic resolution.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
fluorescence; kinetics; molecular dynamics; mutagenesis; nuclear magnetic resonance (NMR); Measles virus; Phosphoproteins; Protein Structure, Tertiary; Viral Proteins; Protein Folding; Biochemistry; Molecular Biology; Cell Biology
Elenco autori:
D. Bonetti, C. Camilloni, L. Visconti, S. Longhi, M. Brunori, M. Vendruscolo, S. Gianni
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