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. 2023 Jun 22;3(7):1902–1910. doi: 10.1021/jacsau.3c00142

Figure 1.

Figure 1

Newly occurring mutations at the β-core region of RBD in the spike protein subjected to mechanical force. (a) Domain architecture of the full-length SARS-CoV-2 spike (S) protein. (b) Sequence alignment of the Omicron variant (BA.1) with the wild-type RBD (333–528). The mutations are highlighted in green or blue. The orange line indicates the four disulfide bonds with the residue number shown. The secondary structure elements of the RBD (PDB code: 6ZGE) are marked with rectangles (helices) and arrows (β-strands) above the sequence. (c) The spike protein trimers (gray) on the SARS-CoV-2 virus particles could bind to ACE2 (light blue) on the human cell surface via the RBDs (orange). (d) Crystal structure of the RBD–ACE2 complex (PDB code: 7wbl). The RBD β-core region and RBM are colored orange and yellow, respectively. Part of ACE2 is represented in light blue. Details of the Omicron variant structure are illustrated in the right panel. Four mutations that first appeared in Omicron are colored green.