Fig. 3 | Signal Transduction and Targeted Therapy

Fig. 3

From: A potent human monoclonal antibody with pan-neutralizing activities directly dislocates S trimer of SARS-CoV-2 through binding both up and down forms of RBD

Fig. 3

Cryo-EM structures of the spike protein S-6P complexed with 35B5 Fab. a The structures of the S-6P-35B5 Fab complex in three states. The S trimer is represented as surface. 35B5 Fab is shown in cartoon and colored in purple. The “down”, “up”, and “releasing” RBD domains are colored in blue, yellow, and red, respectively. The NTD domain of the S trimer is colored in deep gray. The SD1, SD2, and S2 domains are colored in light gray. The gap caused by 35B5 Fab between the “releasing” RBD and NTD domains is highlighted with dashed lines. b Interactions of 35B5 Fab with “up” RBD. The interacting residues within 4 Å in RBD are colored in cyan. The RBD-interacting regions CDRH2, CDRH3, FRH1 and FRH3 of 35B5 Fab are colored in yellow, blue, orange, and red, respectively. c The 35B5 epitope on RBD. The epitope residues are labeled as indicated. d–f Detailed interactions of the CDR (d) and FR regions (e, f) of 35B5 Fab with RBD. Hydrogen-bond and salt-bridge interactions are shown as blue and orange dashed lines, respectively

Back to article page