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[Preprint]. 2023 Jul 5:2023.05.08.539839. Originally published 2023 May 8. [Version 2] doi: 10.1101/2023.05.08.539839

PMC10197565.1; 2023 May 8
PMC10197565.2; 2023 Jul 5

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Figure 7. — Proposed model of the soluble Vpu oligomers. (A) Amino acid sequence of FL Vpu. The linker between Helix 1 and Helix 2 is highlighted in gray, and the residue Q36 is in green. (B) Hexametric arrangement of Vpu monomers: Helices 1 from six protomers come together to form the oligomer core. The linker between Helix 1 and Helix 2, and Helix 2 in each protomer are arranged in a way to stabilize the oligomer. The residues Q36 and N55 are shown as dark green circles. The residue Q36 is possibly oriented toward the oligomer core and occluded. Helix 3 is widely spread and conformationally heterogeneous. Helices 2 and 3 for only three protomers are shown for clarity. Helix 3 is highly dynamic and heterogeneous in conformation—Possible alternative conformations of this Vpu region are shown for just one protomer for the sake of clarity. Also, for the clarity of representation, the model shown here does not account for the possible interactions between Helices 3 from neighboring Vpu protomers.