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Open Access

Correction

Correction: Mouse IgG2c Fc loop residues promote greater receptor-binding affinity than mouse IgG2b or human IgG1

  • The PLOS ONE Staff

The sequences appearing in the lower panel of Fig 1E are not properly aligned due to a technical error. Please see the complete, correct Fig 1 here. The publisher apologizes for the error.

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Fig 1. Mouse IgG2c Fc is comparable to other IgGs but shows differences in crucial features.

A. A cartoon model of mouse IgG2c Fc solved by x-ray crystallography. Domain and secondary structure element labels (B.) are noted. C. An overlay of two mouse IgG2c Fc models with different N-glycan composition. D. A cartoon schematic showing the glycoforms studied here, individual carbohydrate residues are indicated by colored shapes according to the SNFG system [2]. The colors of individual Fcs will be used as indicated throughout the text to denote sequence and glycan variants. E. Sequence and secondary structure arrangement of the Fc Cγ2.

https://doi.org/10.1371/journal.pone.0196609.g001

Reference

  1. 1. Falconer DJ, Barb AW (2018) Mouse IgG2c Fc loop residues promote greater receptor-binding affinity than mouse IgG2b or human IgG1. PLoS ONE 13(2): e0192123. https://doi.org/10.1371/journal.pone.0192123 pmid:29408873

Citation: The PLOS ONE Staff (2018) Correction: Mouse IgG2c Fc loop residues promote greater receptor-binding affinity than mouse IgG2b or human IgG1. PLoS ONE 13(4): e0196609. https://doi.org/10.1371/journal.pone.0196609

Published: April 24, 2018

Copyright: © 2018 The PLOS ONE Staff. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.