pH- and Calcium-Dependent Aromatic Network in the SARS-CoV‑2 Envelope Protein

• Published in: Journal of the American Chemical Society Vol. 144; no. 15; pp. 6839 - 6850
• Main Authors: Medeiros-Silva, João, Somberg, Noah H, Wang, Harrison K, McKay, Matthew J, Mandala, Venkata S, Dregni, Aurelio J, Hong, Mei
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 20.04.2022
• Subjects: calcium; Calcium - metabolism; cations; COVID-19; endoplasmic reticulum; Humans; Hydrogen-Ion Concentration; Ions; Lipids; nuclear magnetic resonance spectroscopy; pathogenicity; peptides; phenylalanine; Protein Conformation; SARS-CoV-2; Severe acute respiratory syndrome coronavirus 2; viruses; Water

The envelope (E) protein of the SARS-CoV-2 virus is a membrane-bound viroporin that conducts cations across the endoplasmic reticulum Golgi intermediate compartment (ERGIC) membrane of the host cell to cause virus pathogenicity. The structure of the closed state of the E transmembrane (TM) domain, E...