File:6xdc SARS-CoV-2 ORF3a.png

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Cryo-electron microscopy structure of the dimeric ORF3a protein from SARS-CoV-2, with the two chains of the dimer in blue and orange. The structure contains three helices per chain that form the transmembrane region, and a C-terminal beta-sheet-rich domain located in the cytosol. The protein can function as an ion channel and is thought to be a viroporin. Rendered using PyMol from PDB: 6XDC​.

Cryo-EM structure of the SARS-CoV-2 3a ion channel in lipid nanodiscs. Kern, D.M., Sorum, B., Mali, S.S., Hoel, C.M., Sridharan, S., Remis, J.P., Toso, D.B., Kotecha, A., Bautista, D.M., Brohawn, S.G. Nature Structural & Molecular Biology volume 28, pages 573–582 (2021)

PubMed: 32587976

DOI: 10.1101/2020.06.17.156554
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Author Opabinia regalis

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current20:52, 11 September 2021Thumbnail for version as of 20:52, 11 September 2021768 × 1,024 (400 KB)Opabinia regalis{{Information |Description=Cryo-electron microscopy structure of the dimeric ORF3a protein from SARS-CoV-2, with the two chains of the dimer in blue and orange. The structure contains three helices per chain that form the transmembrane region, and a C-terminal beta-sheet-rich domain located in the cytosol. The protein can function as an ion channel and is thought to be a viroporin. Rendered using PyMol from {{PDB|6XDC}}. Cryo-EM structure of the SARS-CoV-2 3a ion channel in lipid nanodiscs....
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