The only book to summarize recent achievements in the experimental and computational analyses of structural disorder in viral proteins
Over the past two decades, the hypothesis that protein function relies on precise 3D structure has been challenged by a wealth of counterexamples, showing that many intrinsically disordered proteins (IDPs) function in an entirely or partly disordered state. Despite this large body of experimental evidence of the abundance and biological relevance of IDPs in the living world, the notion of 3D structure is still deeply anchored in many scientists′ minds due mainly to a lack of focus on recent and exciting developments in IDP studies. Flexible Viruses provides the latest information on experimental and computational characterization of structural and functional properties of viral proteins endowed with disordered regions. Featuring chapters by leading research groups around the world, the book contains modern information on various aspects related to the structural and functional roles of intrinsic disorder in viral IDPs. Flexible Viruses:
Addresses debilitating diseases such as AIDS, herpes, lymphoma, and hepatitis
Covers prediction and experimental assessment of disordered regions in partial IDPs
Examines the mechanistic aspects of "folding–coupled–to–binding"
Explains the biological relevance of disordered regions and structural transitions
Analyzes the unique features of each class of viral proteins
Includes case studies from leading research groups around the world
Complete with a detailed presentation of the implications of current findings for new directions in future research and disease management, Flexible Viruses is intended to stimulate and inspire scientists toward further exploration of this intriguing and very promising field.
1. Do viral proteins possess unique features? (Vladimir Uversky).
2. Functional role of structural disorder in capsid proteins (Lars Liljas).
3. Structural disorder within the nucleoproteins and phosphoproteins of measles, Nipah and Hendra viruses (Johnny Habchi and Sonia Longhi).
4. Structural disorder within the Sendai virus nucleoprotein and phosphoprotein (Rob Ruigrok and Martin Blackledge).
5. Structural disorder in Rhabdoviridae phosphoproteins (Marc Jamin).
6. Structural disorder in matrix proteins from HiV–related viruses (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 and oilgomerization–dependent gain of structure (Assaf Friedler).
9. Order from Disorder: Structure, Function and Dynamics of the HIV–1 Transactivator of Transcription (Joe D. O Neil).
10. Intrinsically disordered protein domains of the non structural proteins of Sesbania mosaic virus and their functional role (Handanahal S. Savithri).
11. Intrinsic disorder in genome–linked viral proteins VPgs of potyviruses (Jadwiga Chroboczek, Eugénie Hébrard, Kristiina Mäkinen, Thierry Michon and Kimmo Rantalainen).
12. Intrinsic disorder in HPV 16 E7 protein (Gonzalo de Prat–Gay).
13. The Semiliki forest virus serine protease is disordered and yet displays catalytic activity (Manuel Morillas).
14. Intrinsic disorder in the core proteins of Flaviviridae (Jean–Luc Darlix).
15. Domains 2 and 3 of non–structural protein 5A (NS5A) of hepatitis C virus is natively unfolded (Ho Sup Yoon).
16. Intrinsic disorder within phage N protein and interaction with the E. coli NusA protein (Kristian Schweimer).
17. The N–terminal extension region of Hordeivirus movement TGB1 protein consists of two domains with different content of disordered structure (V.V. Makarov, M.E. Tailansky, E.N. Dobrov, N.O. Kalinina).
VLADIMIR N. UVERSKY is an Associate Professor at the Department of Molecular Medicine at the University of South Florida (USF). He obtained his academic degrees from Moscow Institute of Physics and Technology (PhD in 1991) and from the Institute of Experimental and Theoretical Biophysics, Russian Academy of Sciences (DSc in 1998). He spent his early career working mostly on protein folding at the Institute of Protein Research and Institute for Biological Instrumentation, Russia. In 1998, he moved to the University of California Santa Cruz where for six years he was studying protein folding, misfolding, protein conformation diseases, and protein intrinsic disorder phenomenon. In 2004, he was invited to join the Indiana University School of Medicine as a Senior Research Professor to work on intrinsically disordered proteins. Since 2010, Professor Uversky is with USF, where he continues to study intrinsically disordered proteins and protein folding and misfolding processes. He has authored over 400 scientific publications and edited several books and book series on protein structure, function, folding and misfolding.
SONIA LONGHI is a Director of Research at the Center for the National Scientific Research (CNRS). She obtained her academic degree (PhD) from the University of Milan in 1993. She then went to the Architecture and Function of Biological Macromolecules laboratory (AFMB, UMR 6098, CNRS and Aix–Marseille University) where she did postdoctoral work on protein crystallography. Since 2006, she has been heading the "Structural Disorder and Molecular Recognition" group within the AFMB laboratory. She has authored more than 70 scientific publications and edited a book on measles virus nucleoprotein and coedited, with Prof. Vladimir Uversky, a book entitled Instrumental Analysis of Intrinsically Disordered Proteins (Wiley).