title: Structural disorder within sendai virus nucleoprotein and phosphoprotein: insight into the structural basis of molecular recognition.
abstract: Intrinsically disordered regions of significant length are present throughout eukaryotic genomes, and are particularly prevalent in viral proteins. Due to their inherent flexibility, these proteins inhabit a conformational landscape that is too complex to be described by classical structural biology. The elucidation of the role that conformational flexibility plays in molecular function will redefine our understanding of the molecular basis of biological function, and the development of appropriate technology to achieve this aim remains one of the major challenges for the future of structural biology. NMR is the technique of choice for studying intrinsically disordered proteins, providing information about structure, flexibility and interactions at atomic resolution even in completely disordered proteins. In particular residual dipolar couplings (RDCs) are sensitive and powerful tools for determining local and long-range structural behaviour in flexible proteins. Here we describe recent applications of the use of RDCs to quantitatively describe the level of local structure in intrinsically disordered proteins involved in replication and transcription in Sendai virus.
authors.affiliation: Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CEA-CNRS-UJF, UMR 5075, 41 Rue Jules Horowitz, 38027 Grenoble, France.
authors.forename: Malene Ringkjøbing
authors.initials: MR
authors.lastname: Jensen
authors.forename: Pau
authors.initials: P
authors.lastname: Bernadó
authors.forename: Klaartje
authors.initials: K
authors.lastname: Houben
authors.forename: Laurence
authors.initials: L
authors.lastname: Blanchard
authors.forename: Dominque
authors.initials: D
authors.lastname: Marion
authors.forename: Rob W H
authors.initials: RW
authors.lastname: Ruigrok
authors.forename: Martin
authors.initials: M
authors.lastname: Blackledge
mesh_terms: D006801:Humans; D009698:Nucleoproteins / Q000737:chemistry* / Q000378:metabolism; D010750:Phosphoproteins / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D029082:Sendai virus / Q000737:chemistry* / Q000378:metabolism
chemical_list: D009698:Nucleoproteins; D010750:Phosphoproteins