Figure 1: Crystal structures of Fab m336 in complex with MERS-CoV RBD. | Nature Communications

Figure 1: Crystal structures of Fab m336 in complex with MERS-CoV RBD.

From: Junctional and allele-specific residues are critical for MERS-CoV neutralization by an exceptionally potent germline-like antibody

Figure 1

(a) Complex structure in cartoon representation. Heavy and light chains of m336 are coloured light green and light blue, respectively. The receptor-binding subdomain on MERS-CoV RBD is coloured orange with Trp535 shown in shticks representation. (b) Sequences of m336 heavy chain and light chain with residues that interact with the MERS-CoV RBD highlighted with orange dots. Antibody residues are numbered according to the Kabat nomenclature. (c) Interaction between CDRs of m336 and the MERS-CoV RBD. m336 CDRs are shown in cartoon representation and the MERS-CoV RBD is depicted in semitransparent surface and cartoon. (d) Detailed interactions between m336 and patches 1 and 2 of the MERS-CoV RBD. Key residues are highlighted in stick representation. Hydrogen bonds and salt bridges are displayed with dotted lines connecting interacting atoms. The non-canonical disulphide bond between HCDR3 residues Cys98 and Cys100c is in yellow sticks. Both panels (c,d) are shown as different 90° views from panel (a).

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