The globally devastating effects of COVID19 have created unprecedented urgency among the scientific community, including the uncovering of a number of protein structures in the coronavirus. One of these structures is RNA-dependent RNA polymerase (RdRp), a three part protein responsible for the replication of COVID-19 and the target of the drug remdesivr. It enters the cell as the inactive form RMP, and is converted to the active RTP. Through various interactions and bonds, we can gain some insight into how Remdisivir acts as an adenosine analog, binding to the RNA and terminating chain elongation. This blocks the replication of the coronavirus, and has been proven to shorten recovery time of patients. We can see the similarity between this RdRp molecule and that of other RNA viruses. Observing the interactions of nucleotide analogs such as Remdesivir provide a foundation for developing more potent inhibitors as well as general antiviral inhibitors to treat a wide variety of diseases.
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