Structural characterization of the Man5 glycoform of human IgG3 Fc.

ABSTRACT: Immunoglobulin G (IgG) consists of four subclasses in humans: IgG1, IgG2, IgG3 and IgG4, which are highly conserved but have unique differences that result in subclass-specific effector functions. Though IgG1 is the most extensively studied IgG subclass, study of other subclasses is important to understand overall immune function and for development of new therapeutics. When compared to IgG1, IgG3 exhibits a similar binding profile to Fcγ receptors and stronger activation of complement. All IgG subclasses are glycosylated at N297, which is required for Fcγ receptor and C1q complement binding as well as maintaining optimal Fc conformation. We have determined the crystal structure of homogenously glycosylated human IgG3 Fc with a GlcNAc₂Man₅ (Man5) high mannose glycofor

SUBMITTER: Shah IS 

PROVIDER: S-EPMC5694352 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature