Abstract
A protein’s function is intimately related to its three-dimensional folded structure yet apparently unrelated structures can achieve equivalent functionality. The three distinct families of virus-encoded proteins that inhibit the DNA-repair enzyme uracil-DNA glycosylase by mimicking the appearance of DNA at their surface provide an opportunity to investigate the limits of sequence plasticity. We will use a combination of synthetic gene libraries coupled to an in vivo functional assay, adding insights from structural biology and state-of-the art computation to explore the limits of sequence variation of these inhibitors. Our aims are to evaluate the computational methods and better understand viral evolution.
References
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