Article
Restricted motion of the conserved immunoglobulin G1 N-glycan is essential for efficient FcγRIIIa binding.
Structure (London, England : 1993) - 7 Oct 2014
Subedi Ganesh P, Hanson Quinlin M, Barb Adam W
Abstract excerpt
Immunoglobulin G1 (IgG1)-based therapies are widespread, and many function through interactions with low-affinity Fc γ receptors (FcγR). N-glycosylation of the IgG1 Fc domain is required for FcγR binding, though it is unclear why. Structures of the FcγR:Fc complex fail to explain this because the FcγR polypeptide does not bind the N-glycan. Here we identify a link between motion of the N-glycan and Fc:FcγRIIIa...
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