Structure of human IgM rheumatoid factor Fab bound to its autoantigen IgG Fc reveals a novel topology of antibody—antigen interaction

@article{Corper1997StructureOH,
  title={Structure of human IgM rheumatoid factor Fab bound to its autoantigen IgG Fc reveals a novel topology of antibody—antigen interaction},
  author={Adam L. Corper and Maninder K. Sohi and Vincent R Bonagura and Michael Steinitz and Royston Jefferis and Arnold Feinstein and Dennis Beale and Michael J. Taussig and Brian J. Sutton},
  journal={Nature Structural Biology},
  year={1997},
  volume={4},
  pages={374-381}
}
Rheumatoid factors are the characteristic autoantibodies of rheumatoid arthritis, which bind to the Fc regions of IgG molecules. Here we report the crystal structure of the Fab fragment of a patient-derived IgM rheumatoid factor (RF-AN) complexed with human lgG4 Fc, at 3.2 Å resolution. This is the first structure of an autoantibody–autoantigen complex. The epitope recognised in IgG Fc includes the Cγ2/Cγ3 cleft region, and overlaps the binding sites of bacterial Fc-binding proteins. The… CONTINUE READING
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