Extended Data Fig. 8: SPR binding data for NAbs.
From: SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies
a–c, Kinetic and equilibrium constants for binding to unaltered RBD (indicated as wild type, wt) and mutant RBDs are shown in tables beside structures of a representative NAb–RBD complex for each class. Residues that were mutated are highlighted as coloured side chains on a grey RBD surface. Antibody Vh–Vl domains are shown as cartoons. Kinetic and equilibrium constants for NAbs that contact adjacent RBDs on the S trimer (C144, C002, C119 and C121) do not account for contacts to a secondary RBD because binding was assayed by injected monomeric RBDs over immobilized IgGs. Asterisk indicates kinetic constants determined from a two-state binding model.
