Immunoglobulin G (IgG) Fc receptors play a critical role in linking IgG antibody-mediated
immune responses with cellular effector functions. A high resolution map of the binding site …

The binding sites on human IgG1 for human Fcγ receptor (FcγR) I, FcγRIIa, FcγRIIb, FcγRIIIa
and neonatal FcR have been mapped. A common set of IgG1 residues is involved in binding …

We are investigating the interactions of recombinant human IgG antibodies with Fc receptors
to enable selection of a constant region giving minimal depletion of antigen-bearing cells …

Abstract The Fc variant of IgG2, designated as IgG2σ, was engineered with
V234A/G237A/P238S/H268A/V309L/A330S/P331S substitutions to eliminate affinity for Fcγ …

Interactions between human IgG with human FcγRI and FcγRIIa (R131) were studied to
investigate the role of the hinge region of IgG3 and IgG1 in the binding of the antibodies to …

To characterize the region on human IgG1 responsible for its high-affinity interaction with the
human Fc gamma receptor class I (Fc gamma RI), we have analyzed the binding properties …

Engagement of Fcγ receptors (FcγRs) with the Fc region of IgG elicits immune responses by
leukocytes. The recent crystal structure of FcγRIII in complex with IgG-Fc has provided …

Human IgG subclass proteins exhibit more than 95% primary amino acid sequence
homology in their Fc regions, but each has a unique profile for recognition by the 3 human …

Fcγ receptors (FcγRs) play critical roles in humoral and cellular immune responses through
interactions with the Fc region of immunoglobulin G (IgG). Among them, FcγRI is the only …

The number of studies and the quality of the structural data of Fcγ receptors (FcγRs) has
rapidly increased in the last few years. Upon critical examination of the literature, we have …