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. 2013 Dec 5;289(6):3571–3590. doi: 10.1074/jbc.M113.513366

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© 2014 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 1. — Fc of human IgG1 interacts asymmetrically with FcγRIII. A, representation of the x-ray co-crystal structure of the Fc-FcγRIIIB (Protein Data Bank code 1T83) complex. The FcγRIIIB structure is shown in red; the Fc chain B is shown in blue, and the Fc chain A is shown in green. B, zoomed-in interface between the FcγRIII and left Fc chain B. Contacting residues Leu-235, Ser-239, Asp-265, Leu-328, Pro-329, Ala-330, and Ile-332 are in proximity to the FcγRIII. C, zoomed-in interface between the FcγRIII and right Fc chain A. Contacting residues Leu-235, Gly-236, Pro-238, Ser-239, Asp-265, Ser-267, Asp-270, Tyr-296, Asn-297, Ser-298, Thr-299, and Ala-327 are in proximity to the FcγRIII.