Order and disorder in viral proteins: new insights into an old paradigm. (December 2012)

• Record Type: Journal Article
• Authors: Alves, Carolina; Cunha, Celso
• Is Part Of: Future virology. Volume 7:Number 12(2012)
• Page Start: 1183
• Page End: 1191
• Publication Date: 2012-12
• Subjects: conformational flexibility -- intrinsically disordered protein -- intrinsically disordered region -- intrinsic disorder prediction -- viral protein; Virology -- Periodicals; Virus diseases -- Treatment -- Periodicals; 616.9101
• DOI: 10.2217/fvl.12.114
• Languages: English
• ISSNs: 1746-0794

Abstract

The conventional dogma stating that proteins must fold into a well-defined structure in order to display biological function is being challenged everyday as new data emerge on the relevance of disordered regions and intrinsically disordered proteins. Viral proteins in particular can benefit greatly from the conformational flexibility granted by partially folded or unfolded protein segments. It enables them to adapt to hostile and changing environmental conditions, interact with the required host machinery while evading host defence mechanisms and tolerate the high mutation rates viral genomes are prone to. In this review, we will summarize and discuss the importance of the recent research field of protein disorder that is proving vital to gain better understanding of the roles and functions of viral proteins.