Fig. 2 | Signal Transduction and Targeted Therapy

Fig. 2

From: S19W, T27W, and N330Y mutations in ACE2 enhance SARS-CoV-2 S-RBD binding toward both wild-type and antibody-resistant viruses and its molecular basis

Fig. 2

SARS-CoV-2 S-RBD bound to ACE2 trapped in the closed conformation. a Crystal structure of SARS-CoV-2 S-RBD in complex with ACE2[W19/Y330]. S-RBD is in green and ACE2 subdomains I and II are colored cyan and pale cyan, respectively. W19 and Y330 are highlighted by sticks. b Crystal structure of SARS-CoV-2 S-RBD in complex with ACE2[W27/Y330]. S-RBD is in orange and ACE2 subdomains I and II are colored magenta and light pink, respectively. W27 and Y330 are highlighted by sticks. c Superimposition of the two structures presented in (a) and (b) to highlight the well-aligned S-RBD and ACE2 molecules. d Superimposition of our S-RBD/ACE2[W19/Y330] structure (green for S-RBD, cyan for ACE2 subdomain I, and pale cyan for ACE2 subdomain II) onto a previously reported structure of SARS-CoV-2 S-RBD (yellow) bound to wild-type ACE2 (dark gray for subdomain I and light gray for subdomain II) (PDB code: 6LZG). The movement of ACE2 subdomain I toward subdomain II (by about ~21 Å at the outer edge point) in our structure is highlighted. The subsequent change of the active-site cleft in the two structures is shown in a space-filling mode on the right. e Superimposition of our S-RBD/ACE2[W19/Y330] structure (cyan for subdomain I and pale cyan for subdomain II) onto a previously reported structure of ACE2 (light blue for subdomain I and marine for subdomain II) in complex with the MLN-4760 inhibitor (PDB code: 1R4L). f Dense electron densities for a possible substrate-like peptide observed in the ACE2 active-site cleft in our structures. The electron densities are contoured at 1.5σ using the |Fo|–|Fc| map

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