Oligomeric viral proteins: small in size,large in presence |
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Authors: | Bhargavi Jayaraman Amber M Smith Jason D Fernandes |
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Institution: | 1. Department of Biochemistry and Biophysics, University of California, San Francisco, CA, USA;2. UC Santa Cruz Genomics Institute, Santa Cruz, CA, USA;3. Howard Hughes Medical Institute, University of California, Santa Cruz, CA, USA |
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Abstract: | Viruses are obligate parasites that rely heavily on host cellular processes for replication. The small number of proteins typically encoded by a virus is faced with selection pressures that lead to the evolution of distinctive structural properties, allowing each protein to maintain its function under constraints such as small genome size, high mutation rate, and rapidly changing fitness conditions. One common strategy for this evolution is to utilize small building blocks to generate protein oligomers that assemble in multiple ways, thereby diversifying protein function and regulation. In this review, we discuss specific cases that illustrate how oligomerization is used to generate a single defined functional state, to modulate activity via different oligomeric states, or to generate multiple functional forms via different oligomeric states. |
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Keywords: | Viral proteins oligomeric states multifunctional HIV-1 Capsid Ebolavirus VP40 Flavivirus NS1 HIV-1 Rev |
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