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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1997-05

AUTHORS

A L Corper, M K Sohi, V R Bonagura, M Steinitz, R Jefferis, A Feinstein, D Beale, M J Taussig, B J Sutton

ABSTRACT

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 IgG4 Fc, at 3.2 A resolution. This is the first structure of an autoantibody-autoantigen complex. The epitope recognised in IgG Fc includes the C gamma 2/C gamma 3 cleft region, and overlaps the binding sites of bacterial Fc-binding proteins. The antibody residues involved in autorecognition are all located at the edge of the conventional combining site surface, leaving much of the latter available, potentially, for recognition of a different antigen. Since an important contact residue is somatic mutation, the structure implicates antigen-driven selection, following somatic mutation of germline genes, in the production of pathogenic rheumatoid factors. More... »

PAGES

374-381

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsb0597-374

DOI

http://dx.doi.org/10.1038/nsb0597-374

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1014548963

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9145108


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