| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1014613 |
| landingPage: |
http://www.iedb.org/assay/1649602 |
| type: |
Literature
|
| publicationVenue: |
J Biol Chem
|
| dates: |
1999
|
| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
T Hellmark
H Burkhardt
J Wieslander
|
| method: |
ELISA
|
| name: |
Goodpasture disease. Characterization of a single conformational epitope as the target of pathogenic autoantibodies.
|
| description: |
The discontinuous epitope was mapped using a variety of recombinant NC1 domains constructed by replacing single residues of alpha3(IV) with the corresponding amino acids from the nonreactive alpha1(IV) chain. Replacement mutations were identified that completely destroyed the Goodpasture epitope in the alpha3(IV) chain. The substitution of nine discontinuous positions in the alpha1(IV)NC1 with amino acid residues from the &alpha3 chain resulted in a recombinant construct that was recognized by all patients’ sera but by none of the sera from healthy controls.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |