SARS-CoV-2 is a new virus that has bypassed the world at high speed. Due to its rapid human-to-human transmission, a global pandemic was declared in March 2020. Since people have not yet encountered this virus, it has been questioned what strategies to take to curb the virus and how to ensure successful treatment of the disease called COVID-19 caused by the virus. One of the strategies used is to determine the target site in the virus to which the therapeutic agent can bind. One option is proteins that provide the virus with important functions such as cell entry, aid in viral composition and virus maturation, and viral pathogenesis. Protein E in SARS-CoV-2 is considered as one of the potential therapeutic targets. Given the extensive knowledge of coronaviruses to date, protein E is thought to have similarly important functions as in other coronaviruses, and that its inhibition or elimination can severely weaken the virus. As the smallest structural protein in SARS-CoV-2, it is located in the membrane of the virus and mediates various viral mechanisms and interactions. Its importance is also largely associated with viral pathogenesis. Upon entering the cell, where it is localized primarily to the cell transport regions of the host cell, it has the ability to form a pentameric structure that acts as viroporin in favor of the virus. As a monomer, it comprises three domains: i.) Short hydrophilic N-terminal region, ii.) Hydrophobic transmembrane domain (TMD), and iii.) Long hydrophilic C-terminal region. Some proteins are difficult to isolate and therefore research into their structures and mechanism is difficult. Further research has focused on the use of various techniques and methods to gain a better insight into the structure and understanding of the mechanism of action of SARS-CoV-2 protein E.
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