Immunological Data Discovery Index
Immunological Data Discovery Index
| authorizations: |
registration not required
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| accessURL: |
http://www.iedb.org/reference/1018810 |
| landingPage: |
http://www.iedb.org/assay/1716944 |
| type: |
Literature
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| publicationVenue: |
Nat Struct Biol
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| dates: |
1997
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| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
A L Corper
M K Sohi
V R Bonagura
M Steinitz
R Jefferis
A Feinstein
D Beale
M J Taussig
B J Sutton
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| method: |
surface plasmon resonance (SPR)
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| name: |
Structure of human IgM rheumatoid factor Fab bound to its autoantigen IgG Fc reveals a novel topology of antibody-antigen interaction.
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| description: |
Epitope-specific RF-AN Fab bound IgG with very low affinity, although IgM polyvalency confers enhanced avidity for aggregated IgG (Ka = 2 x 106 M-1) by surface plasmon resonance. In separate experiments, RF-AN Fab bound IgG4, but not IgG3, by ELISA. Substitution of Arg to His of IgG3 matching position 198 of the epitope conferred binding. However, substitution of His to Arg at position 198 of the epitope did not significantly affect binding. The authors conclude that differences in conformation between IgG3 and IgG4 Fc account for the difference in binding. Substitution of Met, Ile, and Ser at positions 15, 16, and 17, respectively, of the epitope abolished binding, confirming that these are critical residues. Note: Residues His198, Met15, Ile16, and Ser17 correspond to residues 435, 252, 253, and 254, respectively, according to the numbering of Kabat et al. (1991) in the reference cited.
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| name: |
iedb
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| homePage: |
http://www.iedb.org |
