Structural Disorder within Paramyxoviral Nucleoproteins and Phosphoproteins in Their Free and Bound Forms: From Predictions to Experimental Assessment
by
Johnny Habchi 1,2 and .JPG)
Sonia Longhi 1,2,*
Johnny Habchi 1,2 and Sonia Longhi 1,2,*
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
Int. J. Mol. Sci. 2015, 16(7), 15688-15726; https://doi.org/10.3390/ijms160715688
Received: 22 May 2015 / Revised: 26 June 2015 / Accepted: 29 June 2015 / Published: 10 July 2015
(This article belongs to the Special Issue In-Silico Prediction and Characterization of Intrinsic Disorder in Proteins)
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
▼
Show Figures
Figure 1
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
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.
Show more citation formats
