Fig. 3: Key residues for binding the hACE2 receptor. | Nature Communications

Fig. 3: Key residues for binding the hACE2 receptor.

From: Structural basis for receptor binding and broader interspecies receptor recognition of currently circulating Omicron sub-variants

Fig. 3

a–c Structural comparisons between Omicron BA.2 and BA.2.12.1 RBDs, BA.2 and BA.2.75 RBDs, or BA.2 and BA.4/5 RBDs. BA.2, BA.2.12.1, BA.2.75, and BA.4/5 RBDs were colored corresponding to Fig. 2a, b. Differential residues between the two variants for comparison were boxed in the dashed lines and shown as sticks in their respective colors. Key residues were also presented as sticks, and those shared by two variants for comparison were labeled in black, except for differential residues, otherwise were labeled with their respective colors. d The binding affinities of the BA.2, BA.4/5 and three BA.4/5 RBD mutants harboring R452L, V486F or R493Q towards the hACE2 receptor. Raw and fitted curves are represented by black and red lines, respectively. KD values shown are the mean ± SD of four independent experiments. e, f The impact of substitutions F486V and R493Q on the interactions between RBD and hACE2. hACE2, BA.2 and BA.4/5 RBDs were colored corresponding to Fig. 2a, b. Source data are provided as a Source Data file.

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