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Int. J. Mol. Sci. 2015, 16(7), 15688-15726; doi:10.3390/ijms160715688

Structural Disorder within Paramyxoviral Nucleoproteins and Phosphoproteins in Their Free and Bound Forms: From Predictions to Experimental Assessment

1
Aix-Marseille Université, Architecture et Fonction des Macromolécules Biologiques (AFMB), UMR 7257, 163, Avenue de Luminy, Case 932, 13288 Marseille, France
2
Centre National pour la Recherche Scientifique (CNRS), AFMB UMR 7257, 163, Avenue de Luminy, Case 932, 13288 Marseille, France
*
Author to whom correspondence should be addressed.
Academic Editor: Lukasz Kurgan
Received: 22 May 2015 / Revised: 26 June 2015 / Accepted: 29 June 2015 / Published: 10 July 2015
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Abstract

We herein review available computational and experimental data pointing to the abundance of structural disorder within the nucleoprotein (N) and phosphoprotein (P) from three paramyxoviruses, namely the measles (MeV), Nipah (NiV) and Hendra (HeV) viruses. We provide a detailed molecular description of the mechanisms governing the disorder-to-order transition that the intrinsically disordered C-terminal domain (NTAIL) of their N proteins undergoes upon binding to the C-terminal X domain (PXD) of the homologous P proteins. We also show that NTAIL–PXD complexes are “fuzzy”, i.e., they possess a significant residual disorder, and discuss the possible functional significance of this fuzziness. Finally, we emphasize the relevance of N–P interactions involving intrinsically disordered proteins as promising targets for new antiviral approaches, and end up summarizing the general functional advantages of disorder for viruses. View Full-Text
Keywords: paramyxoviruses; nucleoprotein; phosphoprotein; intrinsic disorder; induced folding; fuzzy complexes; protein-protein interactions; disorder prediction; molecular recognition elements; antiviral approaches paramyxoviruses; nucleoprotein; phosphoprotein; intrinsic disorder; induced folding; fuzzy complexes; protein-protein interactions; disorder prediction; molecular recognition elements; antiviral approaches
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Habchi, J.; Longhi, S. Structural Disorder within Paramyxoviral Nucleoproteins and Phosphoproteins in Their Free and Bound Forms: From Predictions to Experimental Assessment. Int. J. Mol. Sci. 2015, 16, 15688-15726.

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