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

International Journal of Molecular Sciences

Johnny Habchi¹  Sonia Longhi¹ 

[1] Aix-Marseille Université, Architecture et Fonction des Macromolécules Biologiques (AFMB), UMR 7257, 163, Avenue de Luminy, Case 932, 13288 Marseille, France; E-Mail:

关键词: paramyxoviruses;    nucleoprotein;    phosphoprotein;    intrinsic disorder;    induced folding;    fuzzy complexes;    protein-protein interactions;    disorder prediction;    molecular recognition elements;    antiviral approaches;   

DOI  :  10.3390/ijms160715688

来源: mdpi

【 摘 要 】

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 (N_TAIL) of their N proteins undergoes upon binding to the C-terminal X domain (P_XD) of the homologous P proteins. We also show that N_TAIL–P_XD 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.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.