Figure 6 | Scientific Reports

Figure 6

From: Conformational effects of N-glycan core fucosylation of immunoglobulin G Fc region on its interaction with Fcγ receptor IIIa

Figure 6

Conformational dynamics and rearrangements of Tyr296 of IgG1-Fc. Close-up views of the interaction interface between IgG1-Fc (cyan) and sFcγRIIIa (yellow) are shown: (a) nonfucosylated system; (b) fucosylated system. The representative simulated structures from the nonfucosylated and fucosylated systems, in which the χ1 dihedral angle of Tyr296 exhibited 186° and −55°, respectively, are shown as in Fig. 4(a) and Fig. 4(b), respectively. Sugar residues, Lys128 of sFcγRIIIa, and Asn297 and Tyr296 of IgG1-Fc are shown as sticks, while the fucose residue is colored red. (c) Distribution of χ1 dihedral angles of Tyr296 of IgG1-Fc in nonfucosylated (solid line) and fucosylated (dotted line) systems. Red bar represents the χ1 dihedral angle obtained by crystallographic analysis.

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