Figure 5 | Scientific Reports

Figure 5

From: Assessing the Heterogeneity of the Fc-Glycan of a Therapeutic Antibody Using an engineered FcγReceptor IIIa-Immobilized Column

Figure 5

Binding model. Our data supports that the conformational entropy modulated by galactose governs the binding affinity of IgG to FcγRIIIa. The terminal galactose moiety stabilizes the hinge α-helical peptide located at the interface between the CH2 and CH3 domains. In the presence of N-glycans containing galactose, the CH2 domain remains in a more rigid conformation than that in the agalactosylated G0F glycoform. The rigid conformation yields a less unfavorable entropy change, facilitating the binding to FcγRIIIa. IgG-Fc and FcγRIIIa are represented in gray, and light orange respectively.

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