title: The measles virus N(TAIL)-XD complex: an illustrative example of fuzziness.
abstract: In this chapter, I focus on the biochemical and structural characterization of the complex between the intrinsically disordered C-terminal domain of the measles virus nucleoprotein (N(TAIL)) and the C-terminal X domain (XD) of the viral phosphoprotein (P). I summarize the main experimental data available so far pointing out the prevalently disordered nature of N(TAIL) even after complex formation and the role of the flexible C-terminal appendage in the binding reaction. I finally discuss the possible functional role of these residual disordered regions within the complex in terms of their ability to capture other regulatory, binding partners.
authors.affiliation: Architecture et Fonction des Macromolécules Biologiques, Universités d'Aix-Marseille I et II, Marseille, France. Sonia.Longhi@afmb.univ-mrs.fr
authors.forename: Sonia
authors.initials: S
authors.lastname: Longhi
mesh_terms: D000818:Animals; D006801:Humans; D008459:Measles virus / Q000502:physiology*; D008958:Models, Molecular; D019590:Nucleocapsid Proteins; D009698:Nucleoproteins / Q000737:chemistry* / Q000378:metabolism; D010750:Phosphoproteins / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D019590:Nucleocapsid Proteins; D009698:Nucleoproteins; D010750:Phosphoproteins; D014764:Viral Proteins; C058314:nucleoprotein, Measles virus