Fig. 1: Structural analysis of aRBD-2, aRBD-5, and aRBD-7 binding to the WT SARS-CoV-2 RBD. | Cell Research

Fig. 1: Structural analysis of aRBD-2, aRBD-5, and aRBD-7 binding to the WT SARS-CoV-2 RBD.

From: Hetero-bivalent nanobodies provide broad-spectrum protection against SARS-CoV-2 variants of concern including Omicron

Fig. 1

a–f Three-dimensional structures of aRBD-2 (a, red), aRBD-5 (c, marine) and aRBD-7 (e, green) bound to the SARS-CoV-2 RBD (gray). The overlapped epitope residues between the Nbs and ACE2 on RBD are highlighted in yellow. The interacting residues are shown as sticks in the zoomed-in view of aRBD-2 (b), aRBD-5 (d), and aRBD-7 (f) in complex with RBD, and the hydrogen bonds and salt bridges between the Nbs and RBD are shown as black dotted lines. g The superimposition of the structures of aRBD-2, aRBD-5 and aRBD-7 bound to RBD. h–j The structures of aRBD-2 (h), aRBD-5 (i) and aRBD-7 (j) bound to RBD are also superimposed on that of the RBD:ACE2 complex (PDB ID: 6M0J). The pink circles indicate the clashes between the Nbs and ACE2 (yellow).

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