Flexible Viruses: Structural Disorder in Viral Proteins

The only book to summarize recent achievements in theexperimental and computational analyses of structural disorder inviral proteins

Over the past two decades, the hypothesis that protein functionrelies on precise 3D structure has been challenged by a wealth ofcounterexamples, showing that many intrinsically disorderedproteins (IDPs) function in an entirely or partly disordered state.Despite this large body of experimental evidence of the abundanceand biological relevance of IDPs in the living world, the notion of3D structure is still deeply anchored in many scientists′minds due mainly to a lack of focus on recent and excitingdevelopments in IDP studies. Flexible Viruses provides the latestinformation on experimental and computational characterization ofstructural and functional properties of viral proteins endowed withdisordered regions. Featuring chapters by leading research groupsaround the world, the book contains modern information on variousaspects related to the structural and functional roles of intrinsicdisorder in viral IDPs. Flexible Viruses:

Addresses debilitating diseases such as AIDS, herpes, lymphoma,and hepatitis

Covers prediction and experimental assessment of disorderedregions in partial IDPs

Examines the mechanistic aspects of"folding–coupled–to–binding"

Explains the biological relevance of disordered regions andstructural transitions

Analyzes the unique features of each class of viral proteins

Includes case studies from leading research groups around theworld

Complete with a detailed presentation of the implications ofcurrent findings for new directions in future research and diseasemanagement, Flexible Viruses is intended to stimulate and inspirescientists toward further exploration of this intriguing and verypromising field.

1. Do viral proteins possess unique features? (VladimirUversky).

2. Functional role of structural disorder in capsid proteins(Lars Liljas).

3. Structural disorder within the nucleoproteins andphosphoproteins of measles, Nipah and Hendra viruses (JohnnyHabchi and Sonia Longhi).

4. Structural disorder within the Sendai virus nucleoprotein andphosphoprotein (Rob Ruigrok and Martin Blackledge).

5. Structural disorder in Rhabdoviridae phosphoproteins (MarcJamin).

6. Structural disorder in matrix proteins from HiV–relatedviruses (Vladimir Uversky and Keith Dunker).

7. Structural disorder in proteins from influenza virus(Vladmir Uversky and Keith Dunker).

8. Structural disorder in the HIV–1 Vif protein andoilgomerization–dependent gain of structure (AssafFriedler).

9. Order from Disorder: Structure, Function and Dynamics of theHIV–1 Transactivator of Transcription (Joe D.O Neil).

10. Intrinsically disordered protein domains of the nonstructural proteins of Sesbania mosaic virus and their functionalrole (Handanahal S. Savithri).

11. Intrinsic disorder in genome–linked viral proteins VPgs ofpotyviruses (Jadwiga Chroboczek, Eugénie Hébrard,Kristiina Mäkinen, Thierry Michon and KimmoRantalainen).

12. Intrinsic disorder in HPV 16 E7 protein (Gonzalo dePrat–Gay).

13. The Semiliki forest virus serine protease is disordered andyet displays catalytic activity (Manuel Morillas).

14. Intrinsic disorder in the core proteins ofFlaviviridae (Jean–Luc Darlix).

15. Domains 2 and 3 of non–structural protein 5A (NS5A) ofhepatitis C virus is natively unfolded (Ho Sup Yoon).

16. Intrinsic disorder within phage N protein andinteraction with the E. coli NusA protein (KristianSchweimer).

17. The N–terminal extension region of Hordeivirusmovement TGB1 protein consists of two domains with differentcontent of disordered structure (V.V. Makarov, M.E. Tailansky,E.N. Dobrov, N.O. Kalinina).

VLADIMIR N. UVERSKY is an Associate Professor at the Departmentof Molecular Medicine at the University of South Florida (USF). Heobtained his academic degrees from Moscow Institute of Physics andTechnology (PhD in 1991) and from the Institute of Experimental andTheoretical Biophysics, Russian Academy of Sciences (DSc in 1998).He spent his early career working mostly on protein folding at theInstitute of Protein Research and Institute for BiologicalInstrumentation, Russia. In 1998, he moved to the University ofCalifornia Santa Cruz where for six years he was studying proteinfolding, misfolding, protein conformation diseases, and proteinintrinsic disorder phenomenon. In 2004, he was invited to join theIndiana University School of Medicine as a Senior ResearchProfessor to work on intrinsically disordered proteins. Since 2010,Professor Uversky is with USF, where he continues to studyintrinsically disordered proteins and protein folding andmisfolding processes. He has authored over 400 scientificpublications and edited several books and book series on proteinstructure, function, folding and misfolding.

SONIA LONGHI is a Director of Research at the Center for theNational Scientific Research (CNRS). She obtained her academicdegree (PhD) from the University of Milan in 1993. She then went tothe Architecture and Function of Biological Macromoleculeslaboratory (AFMB, UMR 6098, CNRS and Aix–Marseille University)where she did postdoctoral work on protein crystallography. Since2006, she has been heading the "Structural Disorder and MolecularRecognition" group within the AFMB laboratory. She has authoredmore than 70 scientific publications and edited a book on measlesvirus nucleoprotein and coedited, with Prof. Vladimir Uversky, abook entitled Instrumental Analysis of Intrinsically DisorderedProteins (Wiley).