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Article Dans Une Revue Journal of Biological Chemistry Année : 2016

Identification and Structural Characterization of an Intermediate in the Folding of the Measles Virus X Domain

Daniela Bonetti
  • Fonction : Auteur
Carlo Camilloni
  • Fonction : Auteur
Lorenzo Visconti
  • Fonction : Auteur
Maurizio Brunori
  • Fonction : Auteur
Michele Vendruscolo
  • Fonction : Auteur
Stefano Gianni

Résumé

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.
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hal-01439066 , version 1 (11-07-2024)

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Daniela Bonetti, Carlo Camilloni, Lorenzo Visconti, Sonia Longhi, Maurizio Brunori, et al.. Identification and Structural Characterization of an Intermediate in the Folding of the Measles Virus X Domain. Journal of Biological Chemistry, 2016, 291 (20), pp.10886+. ⟨10.1074/jbc.M116.721126⟩. ⟨hal-01439066⟩
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