Abstract
As the link between antigen binding and immune activation, the antibody Fc region has received extensive structural study. In this report, the structure of the Fc fragment of the NIST IgG1 mAb (reference material 8671) is described at 2.1 Å resolution in space group P212121, with approximate unit-cell parameters a= 50, b = 80, c = 138 Å. Prior Fc structures with a wide variety of modifications are also surveyed, focusing on those in the same crystal form. To facilitate the analysis of conformations, a reference frame and a two-parameter metric are proposed, considering the CH2 domains as mobile with respect to a fixed dimeric CH3 core. Over several human Fc structures, a significant variation in Fc elbow conformations is observed, which may serve to facilitate the regulation of Fc effector signaling.
Highlights
IntroductionThe Fc (fragment crystallizing) of the IgG antibody was named by Rodney Porter, who found that it crystallized unexpectedly in his refrigerator (Porter, 1959)
The Fc of the IgG antibody was named by Rodney Porter, who found that it crystallized unexpectedly in his refrigerator (Porter, 1959)
To provide a scientific description of this material and to facilitate its application, we report the crystal structure of its Fc fragment
Summary
The Fc (fragment crystallizing) of the IgG antibody was named by Rodney Porter, who found that it crystallized unexpectedly in his refrigerator (Porter, 1959). The Protein Data Bank (Berman et al, 2000) contains over 100 structures of human IgG Fc crystallized with variations in the glycan, in the protein sequence and in the crystallization conditions, and in various complexes (see Supplementary Table S1 for a summary of precedent Fc structures). The set of uncomplexed human Fc structures includes one common recurring crystal form in space group P212121, with approximate unit-cell parameters a = 50, b = 80, c = 138 A. This common crystal includes about 40 structures, but for
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