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. 2018 Apr 24;9:865. doi: 10.3389/fimmu.2018.00865

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Copyright © 2018 Morgan, Holzer, Hemmink, Salguero, Schwartz, Agatic, Cameroni, Guarino, Porter, Rijal, Townsend, Charleston, Corti and Tchilian.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Putative amino acid sequence alignment of FcγR and IgG subclasses. (A) Second IgG domain of human, mouse, and pig Fcγ receptors. (B) Lower hinge and CH2 domain of human, mouse, and pig IgG subclasses. Previously reported Fc-FcγR contact sites are shaded. Beta-strands are labeled and shown at top. (C) Left. Model of the interaction of the Fc region of human IgG1 (green) with human FcgRIIIb (light blue) (pdb, 1t83). Fc-bound glycans are shown as orange spheres. The L234 and L235 Fc residues (purple) and the G159 residue of the FcγRIIIb FG loop are identified. Right. Modeling of the positioning of the porcine K159 residue in the FG loop and its clash with the Fc residue L235.