| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1014701 |
| landingPage: |
http://www.iedb.org/assay/1644995 |
| type: |
Literature
|
| publicationVenue: |
Proc Natl Acad Sci U S A
|
| dates: |
1992
|
| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
S E Artandi
K L Calame
S L Morrison
V R Bonagura
|
| method: |
ELISA
|
| name: |
Monoclonal IgM rheumatoid factors bind IgG at a discontinuous epitope comprised of amino acid loops from heavy-chain constant-region domains 2 and 3.
|
| description: |
The residues important for monoclonal RF binding to IgG4 were deduced by analyzing reactivity with mutated chimeric IgG. The 15 monoclonal RF bind IgG4, as well as IgG1 and IgG2, but not IgG3. Substitution of Arg to His at residue 435 in a non-binding IgG4-IgG3 chimeric molecule resulted in strong binding. This residue is in the CH3 domain. Substitution of residues Met-Ile-Ser at 252-254 and Leu-His-QGln at 309-311 with Gly or Pro residues eliminated RF binding for 14 of 15 and 10 of 15, respectively, monoclonal RF. The authors conclude that these residues, in loops connecting beta-strands at the CH2- CH3 interface, are important residues for RF binding. Polyclonal RF reacted similarly to the monoclonal RF.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |