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The molecular specificity of IgG-Fc interactions with Fcγ receptors

  • Yusuke Mimura
  • Rodolfo Ghirlando
  • Peter Sondermann
  • John Lund
  • Roy Jefferis
Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 495)

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.

Keywords

Molecular Specificity Effector Ligand Ligand Stoichiometry Influence Protein Structure Effector Function Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 2001

Authors and Affiliations

  • Yusuke Mimura
    • 1
  • Rodolfo Ghirlando
    • 2
  • Peter Sondermann
    • 3
  • John Lund
    • 1
  • Roy Jefferis
    • 1
  1. 1.Division of Immunity and InfectionThe Medical SchoolBirminghamUK
  2. 2.LMB-NIDDK-NIHBethesdaUSA
  3. 3.Max-Planck InstituteMartinsriedGermany

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