Immunological Data Discovery Index
Immunological Data Discovery Index
| authorizations: |
registration not required
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| accessURL: |
http://www.iedb.org/reference/1014570 |
| landingPage: |
http://www.iedb.org/assay/1658569 |
| type: |
Literature
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| publicationVenue: |
J Mol Biol
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| dates: |
2007
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| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
Stephane Duquerroy
Enrico A Stura
Sté
phane Bressanelli
Stella M Fabiane
Marie C Vaney
Dennis Beale
Maureen Hamon
Paolo Casali
Felix A Rey
Brian J Sutton
Michael J Taussig
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| method: |
ELISA
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| name: |
Crystal structure of a human autoimmune complex between IgM rheumatoid factor RF61 and IgG1 Fc reveals a novel epitope and evidence for affinity maturation.
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| description: |
The epitope is located on both (identical) chains of the antigen. The epitope residues are T233, G303, V305, Q321, K322, S323, L324, S325 of one chain in [Swiss-Prot: P01857], which correspond to the residues T350, G420, V422, Q438, K439, S440, L441, S442 of chain A in [PDB: 2J6E], and R238, D239, T242, K297, Q301 of the second chains in [Swiss-Prot: P01857], which correspond to the residues R355, D356, T359, K414, Q418 of chain B in [PDB: 2J6E].
The binding of the epitope-specific monoclonal IgM rheumatoid factor RF61 to human IgG(kappa) molecules was tested. Its specificity is for IgG1, −2, and −3, with ∼10-fold lower affinity for IgG4. RF61 binding to human IgG is not subject to inhibition by Staphylococcus aureus protein A.
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| name: |
iedb
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| homePage: |
http://www.iedb.org |
