User:Mattiascollin/IgG sandbox

Here I will draft material for revising the page Immunoglobulin G

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Structure[edit]
Immunoglobulin G (IgG) antibodies are globular proteins with a molecular weight of about 150 kDa made of four peptide chains. It contains two identical class γ heavy chains of about 50 kDa and two identical light chains of about 25 kDa, thus a tetrameric quaternary structure. The two heavy chains are linked to each other and to a light chain each by disulfide bonds. The resulting tetramer has two identical halves, which together form the Y-like shape. Each end of the fork contains an identical antigen binding site. The various regions and domains of a typical IgG are depicted in the figure to the left. Each heavy chain contains a conserved N-glycosylation site at an asparagine residue in the Fc portion of IgG. The N-glycans attached to this site are predominantly core-fucosylated biantennary structures of complex type. (Figure?) In addition, small amounts of these N-glycans also bear bisecting GlcNAc and α-2,6-linked sialic acid residues. The N-glycan composition in IgG has been linked to several autoimmune, infectious and metabolic diseases.