Fig. 3: Conformational response of FcRn to H-mAb or C-mAb binding. | Communications Biology

Fig. 3: Conformational response of FcRn to H-mAb or C-mAb binding.

From: Identification of a direct interaction between the Fab domains of IgG antibodies and human FcRn upon IgG-FcRn complex formation

Fig. 3

A Differential HDX results mapped onto the crystal structure of FcRn (α-domain: pale green, β2m: light pink, PDB ID: 4N0U). Regions in the α domain and β2m displaying a significant protection from exchange in the presence of H-mAb or C-mAb are colored orange and red, respectively. Regions displaying a significant deprotection from exchange in the presence of H-mAb or C-mAb are colored blue, while regions for which no HDX information could be obtained are colored gray. B–E HDX uptake plots of selected peptides. HDX is plotted as a function of time for FcRn (gray curves), FcRn in the presence of C-mAb (red curves), and FcRn in the presence of H-mAb (blue curves). Maximally labeled (90%) FcRn samples are plotted as purple spheres at the longest time point. Single values are shown as spheres, the mean is shown as a long horizontal line, and the SD is plotted as error bars. An asterisk marks time points with a significant difference in HDX (n = 3 for all data points, except the last four time points of FcRn in the presence of H-mAb, where n = 1).

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