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[Preprint]. 2020 Jul 1:2020.07.01.182659. [Version 1] doi: 10.1101/2020.07.01.182659

Figure 5.

Figure 5

Conformational changes of ACE2 upon SARS-CoV-2 binding. A) apo structure of ACE2 (PDB ID: 1R42).The N-terminal subdomain was colored in cyan with the secondary structures of SARS-CoV-2 spike binding sites highlighted in blue. The C-terminal domain of apo ACE2 was colored in wheat. All subsequent structural superpositions were based the alignment of ACE2 residues 20–84 that formed the first 2 helix for RBD domain interaction. The ACE2 inhibitor MLN-4760 (purple) and Angiotensin II (yellow) were positioned in the substrate pocket based on the structural alignment. B) ACE2 structure with inhibitor MLN-4760 binding (PDB ID: 1R4L). The C-terminal domain was highlighted in orange. C) hACE in complex with Ang II(PDB ID: 4APH). The C-terminal domain was highlighted in orange. D)ACE2 structure in complex with SARS-CoV RBD(PDB ID: 2AJF). The C-terminal domain was highlighted in yellow. E) ACE2 structure in complex with SARS-CoV-2 RBD (PDB ID: 6M0J). The C-terminal domain was highlighted in lime green. F) ACE2 structure in complex with a chimeric SARS-CoV-2 RBD domain (PDB ID: 6VW1). The C-terminal domain was highlighted in green. G) Enlarged view of ACE2 substrate binding pocket. One additional ACE2-SARS-CoV-2 RBD complex(PDB ID: 6LZG) was included. The residue color scheme was listed in the bottom panel.