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

[This corrects the article DOI: 10.1371/journal.pone.0192123.].

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.

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.