Fig. 3: Protein-glycan contacts at the nanobody-IgG binding interface.
From: Mechanism of glycoform specificity and in vivo protection by an anti-afucosylated IgG nanobody
a Schematic of the highly conserved N-glycan at IgG Fc N297. Residues colored and numbered according to SNFG standards. Residues with solid outline are part of the core Man3GlcNAc4 motif, while those with dashed outlines are variable. b X0 CDR3 loop contacts the Fc glycan. Hydrogen bonds are shown by dashed black lines. IgG1 as transparent surface (purple), X0 as cartoon (teal), and glycan as sticks with heteroatoms shown (yellow). Relevant X0 residues highlighted in shades of blue. c The X0 CDR3-Fc glycan interface with the core fucose (red sticks with transparent surface) modeled in from 3AVE to reveal potential clashes. d Log2 fold change in KD of X0 T101 mutants. Horizontal dashed line represents the KD of the wildtype X0-Fc interaction. Source data are provided as a Source Data file.
