Fig. 3: Structure of SARS-CoV-2 envelope protein’s transmembrane ___domain in ERGIC-mimetic lipid bilayers. | Nature Structural & Molecular Biology

Fig. 3: Structure of SARS-CoV-2 envelope protein’s transmembrane ___domain in ERGIC-mimetic lipid bilayers.

From: Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane ___domain in lipid bilayers

Fig. 3

a, Ensemble of ten lowest-energy structures. b, Side view of the most representative structure together with the HOLE-calculated pore water (gray). Pore-lining residues are shown as sticks. c, Simplified two-helix view with the pore-facing residues and their distributions in the lowest-energy ensemble. d, Pore radius of ETM obtained from the HOLE program. e–h, Additional snapshots from the most representative structure. e, Lipid-facing and helix-interface positions of the three Phe residues. f, Two clusters of methyl-interdigitating Leu, Ile and Val residues, stabilizing the helix–helix interface. g, Top views of the N-terminal Glu8, the pore-facing Asn15, and the three Phe residues. h, Surface plots of the pentamer, showing the N- and C-terminal vestibules where Asn15 and Lys28 are the first pore-facing residue.

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