Abstract
ORF7b is a 43-amino-acid single-pass transmembrane protein that is associated with the virulence of SARS-CoV-2 and localizes to the endoplasmic reticulum-Golgi intermediate compartment. Its homodimer associates to suppress host immune response; however, a structural model of protein-protein interface within the homodimer is unknown. This work aims to investigate the ORF7b homodimerization through molecular dynamics (MD) and provide insights into molecular interactions to assist the design of inhibitions.
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