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. 2022 Nov 1;54(11):1850–1861. doi: 10.1038/s12276-022-00870-5

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© The Author(s) 2022

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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Fig. 3 — a The combinatorial effects of the two mutations (Q311R and M428L) of PFc29 on hFcRn binding. For the FACS analysis, E. coli spheroplasts displaying an Fc variant (wild-type Fc, Fc-428L, Fc-Q311R, or Fc-PFc29) were labeled with 40 nM hFcRn-SA-Alexa 488 at pH 6.0 and pH 7.4. The mean fluorescence intensities (MFIs) resulting from the FACS analysis are represented as a bar graph. Error bars indicate the standard deviations calculated from triplicate samples. b Superposition of two complex model structures, hFcRn (green)/Fc-M428L (blue) and hFcRn (yellow)/wild-type Fc (white). To examine how the M428L mutation affects the distance between the Fc region and hFcRn, the two complex models (hFcRn/Fc-M428L and hFcRn/wild-type Fc) are superposed based on hFcRn C^α, and a zoomed-in view showing the interaction between hFcRn and the 250-helix region (residues K246–M252) is outlined with a thick line box. The bidirectional arrow in the box indicates the structural distance between Fc-M428L (blue) and wild-type Fc (gray), and the side chain of the M428L residue of Fc-428L is shown in stick representation (purple). c Molecular complex model of PFc29/hFcRn. PFc29, hFcRn α-chain, and β2-microglobulin are colored cyan, yellow, and green, respectively. A contact area close to Q311R is indicated by a box, and electrostatic interactions (Q311R_PFc29–E138_hFcRn or Q311R_PFc29–E139_hFcRn) are represented by dashed lines.