Fig. 5: Structural basis of the competitive binding of h11B11 and RBDs with hACE2.
From: A broadly neutralizing humanized ACE2-targeting antibody against SARS-CoV-2 variants
a The overall structure of h11B11-Fab and hACE2. The Fab is shown as the surface with HCDR1, HCDR2, and HCDR3 from the heavy chain (cyan) colored in red, orange, and purple, while the LCDR1, LCDR2, and LCDR3 from light chain (pink) are colored in blue, green, and gray, respectively. The hACE2 is shown as a cartoon. The N-terminal helix (NTH) is marked by a dotted line. b Superimposition of h11B11/hACE2 complex and HCoV-NL63-RBD/hACE2 (PDB:3KBH), SARS-CoV-RBD/hACE2 (PDB:2AJF), and SARS-CoV-RBD/hACE2 (PDB:6LZG) reveal the competition between h11B11 and RBDs. The ACE2, HCoV-NL63-RBD, SARS-CoV-RBD, and SARS-CoV-RBD are colored differently as indicated. c–e Competitive binding surfaces of h11B11 and RBDs on hACE2. The overlapping epitopes bound by both h11B11 and RBDs are colored in purple. The surfaces in contact with MAb are colored in yellow, while others in contact with RBDs are colored differently as indicated.
