Flexible Viruses Structural Disorder in Viral Proteins

by Uversky, Vladimir; Longhi, Sonia

• ISBN13: 9780470618318
• ISBN10: 0470618310
• Edition: 1st
• Format: Hardcover
• Copyright: 2012-02-07
• Publisher: Wiley

Summary

This book provides up-to-date information on experimental and computational characterization of the structural and functional properties of viral proteins, which are widely involved in regulatory and signaling processes. With chapters by leading research groups, the book features current information on the structural and functional roles of intrinsic disorders in viral proteomes. It systematically addresses the measles, HIV, influenza, potato virus, forest virus, bovine virus, hepatitis, and rotavirus as well as viral genomics. After analyzing the unique features of each class of viral proteins, future directions for research and disease management are presented.

Author Biography

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).

Table of Contents

Preface	p. ix
Introduction to the Wiley Series on Protein and Peptide Science	p. xv
Contributors	p. xvii
Do Viral Proteins Possess Unique Features?	p. 1
Functional Role of Structural Disorder in Capsid Proteins	p. 35
Structural Disorder Within the Nucleoprotein and Phosphoprotein from Measles, Nipah, and Hendra Viruses	p. 47
Structural Disorder Within Sendai Virus Nucleoprotein and Phosphoprotein	p. 95
Structural Disorder in Proteins of the Rhabdoviridae Replication Complex	p. 115
Structural Disorder in Matrix Proteins of HIV-Related Viruses	p. 143
Structural Disorder in Proteins From Influenza Virus	p. 169
Making Order in the Intrinsically Disordered Regions of HIV-1 Vif Protein	p. 201
Order from Disorder: Structure, Function, and Dynamics of the HIV-1 Transactivator of Transcription	p. 223
Intrinsically Disordered Domains of Sesbania Mosaic Virus Encoded Proteins	p. 257
Intrinsic Disorder in Genome-Linked Viral Proteins VPgs of Potyviruses	p. 277
Intrinsic Disorder in the Human Papillomavirus E7 Protein	p. 313
The Semliki Forest Virus Capsid Protease is Disordered and Yet Displays Catalytic Activity	p. 347
Core-lations Between Intrinsic Disorder and Multifaceted Activities in Hepatitis C Virus and Related Viruses	p. 375
The NS5A Domain II of HCV: Conservation of Intrinsic Disorder in Several Genotypes	p. 409
Bacteriophage ¿ N Protein Disorder-Order Transitions Upon Interactions with RNA or Proteins	p. 425
N-Terminal Extension Region of Hordeivirus Movement TGB1 Protein Consists of Two Domains with Different Content of Disordered Structure	p. 445
Index	p. 473
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