title: Order and Disorder in the Replicative Complex of Paramyxoviruses.
abstract: In this review we summarize available data showing 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 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 P proteins. We also show that a significant flexibility persists within NTAIL-XD complexes, which therefore provide illustrative examples of "fuzziness". The functional implications of structural disorder for viral transcription and replication are discussed in light of the ability of disordered regions to establish a complex molecular partnership and to confer a considerable reach to the elements of the replicative machinery.
authors.affiliation: Aix-Marseille Université, AFMB UMR 7257, 13288, Marseille, France.|CNRS, AFMB UMR 7257, 13288, Marseille, France.
authors.forename: Jenny
authors.initials: J
authors.lastname: Erales
authors.affiliation: Aix-Marseille Université, AFMB UMR 7257, 13288, Marseille, France.|CNRS, AFMB UMR 7257, 13288, Marseille, France.
authors.forename: David
authors.initials: D
authors.lastname: Blocquel
authors.affiliation: Aix-Marseille Université, AFMB UMR 7257, 13288, Marseille, France.|CNRS, AFMB UMR 7257, 13288, Marseille, France.
authors.forename: Johnny
authors.initials: J
authors.lastname: Habchi
authors.affiliation: Aix-Marseille Université, AFMB UMR 7257, 13288, Marseille, France.|CNRS, AFMB UMR 7257, 13288, Marseille, France.
authors.forename: Matilde
authors.initials: M
authors.lastname: Beltrandi
authors.affiliation: Aix-Marseille Université, AFMB UMR 7257, 13288, Marseille, France.|CNRS, AFMB UMR 7257, 13288, Marseille, France.
authors.forename: Antoine
authors.initials: A
authors.lastname: Gruet
authors.affiliation: Aix-Marseille Université, AFMB UMR 7257, 13288, Marseille, France.|CNRS, AFMB UMR 7257, 13288, Marseille, France.
authors.forename: Marion
authors.initials: M
authors.lastname: Dosnon
authors.affiliation: Aix-Marseille Université, AFMB UMR 7257, 13288, Marseille, France.|CNRS, AFMB UMR 7257, 13288, Marseille, France.
authors.forename: Christophe
authors.initials: C
authors.lastname: Bignon
authors.affiliation: Aix-Marseille Université, AFMB UMR 7257, 13288, Marseille, France. Sonia.Longhi@afmb.univ-mrs.fr.|CNRS, AFMB UMR 7257, 13288, Marseille, France. Sonia.Longhi@afmb.univ-mrs.fr.
authors.forename: Sonia
authors.initials: S
authors.lastname: Longhi
mesh_terms: D064267:Intrinsically Disordered Proteins / Q000737:chemistry*; D010252:Paramyxoviridae / Q000737:chemistry* / Q000502:physiology*; D011487:Protein Conformation; D014764:Viral Proteins / Q000737:chemistry*; D014779:Virus Replication
chemical_list: D064267:Intrinsically Disordered Proteins; D014764:Viral Proteins
keywords: Folding upon binding; Hedra virus; Intrinsic disorder; Measles virus; Nipah virus; Viral proteins