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. 2018 Mar 2;8:3955. doi: 10.1038/s41598-018-22199-8

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Comparison of structures of glycosylated and non-glycosylated FcγRIIIa in complex with IgG-Fc. (a) Crystal structure of Fc-FcγRIIIa complex. Recombinant Mut FcγRIIIa was expressed in Escherichia coli (non-glycosylated, left panel). (b) Previously reported crystal structure of Fc-FcγRIIIa complex (right panel, PDB ID: 3SGJ). Non-glycosylated FcγRIIIa, glycosylated FcγRIIIa, Fc, and the glycan attached to Fc are depicted in orange, light green, cyan, and magenta, respectively. The N-glycan molecule attached to Asn168 of FcγRIIIa is depicted in yellow sticks. The letters A, B, and C represent chains A and B of Fc, and FcγRIIIa, respectively. (c) Buried surface area (Å²) calculated by the PISA server⁵¹. GA, GB, GC indicate the N-glycan attached to Fc (chain A), Fc (chain B), and FcγRIIIa, respectively. The asterisks indicate that no interaction is possible for the non-glycosylated FcγRIIIa produced in E. coli.