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![[Figure 1]](cb5127fig1mag.jpg)
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Figure 1
NMR work by the Torres group led to early models of the monomeric form of the SARS-CoV E protein in detergent–lipid micelles (Li et al., 2014  ), showing two helical segments joined by a more disordered flexible region flanked by amino-acid residues Tyr42 and Thr55 (a). The N-terminal portion of the TM region [indicated by residue Val14 in (a)] is purported to protrude into the lumenal side of the Golgi membranes, and the C-terminal portion (here indicated by Asn64) to be partly exposed to the cytoplasm. (b) Subsequent work showed the calculated E monomers to consist of three α-helical segments in LMPG micelles. The model shown corresponds to an ensemble of ten calculated monomeric structures, with the backbone rendered as a line representation. Reproduced from Surya et al. (2018) with permission from Elsevier Masson SAS under the Creative Commons Attribution licence (https://creativecommons.org/licenses/by/4.0). |
![[Figure 1]](cb5127fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
