Abstract
The molecular specificity and mechanisms for the interaction of immunoglobulins with Fc binding ligands has been a subject of intensive investigation for many years. Significant information has been gained for human IgG-Fc from x-ray crystallographic analysis of IgG-Fc and IgGFc/ligand complexes. The crystal complexes of IgG-Fc with FcRn, SpA, SpG and rheumatoid factor autoantibody ligands revealed binding sites at the CH2/CH3 interface and an IgG-Fc:ligand stoichiometry of 1:2; reflecting the two fold symmetry of the IgG molecule [1]. For FcγR and C 1 q monomeric IgG must necessarily be functionally monovalent since IgG, FcγR bearing cells and Cl co-exist in the blood, in the absence of activation and the consequent inflammatory reactions.
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Mimura, Y., Ghirlando, R., Sondermann, P., Lund, J., Jefferis, R. (2001). The molecular specificity of IgG-Fc interactions with Fcγ receptors. In: Mackiewicz, A., Kurpisz, M., Żeromski, J. (eds) Progress in Basic and Clinical Immunology. Advances in Experimental Medicine and Biology, vol 495. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0685-0_7
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DOI: https://doi.org/10.1007/978-1-4615-0685-0_7
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