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. 2023 Nov 22;12:e74060. doi: 10.7554/eLife.74060

Figure 1. Identification of residue 417 as a molecular switch that regulates the conformation of SARS-CoV-2 spike.

Figure 1.

(A) Structure of trimeric SARS-CoV-2 spike ectodomain in the closed conformation with three receptor-binding domains (RBDs) down (PDB 6VXX). Each monomeric subunit of the spike trimer is colored differently. The RBD contains a core structure (in cyan) and a receptor-binding motif (RBM; in magenta). Lys417 in the RBD is shown as blue sticks. (B) A hydrogen bond is formed between the side chain of Lys417 from one spike subunit and the main chain of Asn370 from another spike subunit, stabilizing the trimeric spike in the closed conformation. (C) Residue 417 is a valine in SARS-CoV-1 spike and has been a mutational hotspot in later SARS-CoV-2 variants.