title: Structural disorder within paramyxoviral nucleoproteins.
abstract: In this review I summarize available data pointing to the abundance of structural disorder within the nucleoprotein (N) from three paramyxoviruses, namely the measles (MeV), Nipah (NiV) and Hendra (HeV) viruses. I provide a detailed description of the molecular mechanisms that govern 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 (XD) of the homologous phosphoproteins. I also show that a significant flexibility persists within NTAIL-XD complexes, which makes them illustrative examples of "fuzziness". Finally, I discuss the functional implications of structural disorder for viral transcription and replication in light of the promiscuity of disordered regions and of the considerable reach they confer to the components of the replicative machinery.
authors.affiliation: Aix-Marseille Université, AFMB UMR 7257, 13288 Marseille, France; CNRS, AFMB UMR 7257, 13288 Marseille, France. Electronic address: Sonia.Longhi@afmb.univ-mrs.fr.
authors.forename: Sonia
authors.initials: S
authors.lastname: Longhi
mesh_terms: D045404:Hendra Virus / Q000378:metabolism; D064267:Intrinsically Disordered Proteins / Q000737:chemistry* / Q000378:metabolism; D008459:Measles virus / Q000378:metabolism; D008958:Models, Molecular; D045405:Nipah Virus / Q000378:metabolism; D019590:Nucleocapsid Proteins / Q000737:chemistry* / Q000378:metabolism; D018583:Pliability; D011485:Protein Binding; D017510:Protein Folding; D017434:Protein Structure, Tertiary
chemical_list: D064267:Intrinsically Disordered Proteins; D019590:Nucleocapsid Proteins
keywords: Fuzzy complex; Induced folding; Intrinsic disorder; Nucleoprotein; Paramyxovirus; Protein–protein interaction