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. 2018 May 14;9:1884. doi: 10.1038/s41467-018-04271-z

Fig. 3.

Fig. 3

Structure of a JUNV GP1 ternary Fab complex. a Ribbon diagram of JUNV GP1 (red) bound to CR1-10 (heavy chain in cyan, light chain in gray) and CR1-28 (heavy chain in purple, light chain in gray) Fabs. The antibody CDRs and GP1 segments involved in interactions are labeled. L: loop. LC: light chain. HC: heavy chain. A site of N-linked glycosylation at Asn178 (for which we observed interpretable density) is shown. Disulfides are shown as yellow sticks. b Overlay of the JUNV GP1/GD01 Fab structure (PDB: 5EN2)14 with the JUNV GP1/CR1-28 Fab subcomplex. The difference in the angle of Fab approach (from the perspective of the variable domain) is indicated and is similar for all copies in the ASU. The side chain for a tyrosine that is conserved in the CDR H3 of both antibodies is shown as sticks and indicated with an arrow. c Surface representation of GP1 (red) with interacting segments of CR1-28 CDR H3 (leftmost panel), GD01 CDR H3 (PDB: 5EN2,14 middle panel), or the TfR1 βII-2 strand (PDB: 3KAS,13 rightmost panel) shown in cartoon representation. Residues that line the Tyr211TfR1 pocket are shown in cyan and labeled—the residue that lines the back of the GP1 pocket is indicated with a curved arrow. The tyrosine side chain that occupies the GP1 pocket in each instance is shown as sticks and is indicated with an asterisk