| identifier: | 1823138 |
| description: |
epitope description:H: Y33, D52, E53, Q54, N56, I58, D95, T96, A97, A98, Y99; L: R27, D28, I29, K30, Y32, Y49, Y50, S53, H91, G92, E93, S94, W96
antigen name:Immunoglobulin
host organism:Mus musculus BALB/c
antibody name:6A6
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
12888350 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1018807 |
| landingPage: |
http://www.iedb.org/assay/1823138 |
| type: |
Literature
|
| publicationVenue: |
J Mol Biol
|
| dates: |
2003
|
| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
Charles Eigenbrot
Y Gloria Meng
Rajeswari Krishnamurthy
Michael T Lipari
Leonard Presta
Brigitte Devaux
Terence Wong
Paul Moran
Sherron Bullens
Daniel Kirchhofer
|
| method: |
ELISA
|
| name: |
Structural insight into how an anti-idiotypic antibody against D3H44 (anti-tissue factor antibody) restores normal coagulation.
|
| description: |
The epitope residues are calculated from the PDB structure [PDB: 1PG7] as the antigen residues at 4 Å
distance from the antibody.
Epitope-specific anti-idiotope Fab 6A6 bound equally to Fab D3H44 or to a chimeric Fab with the murine D3 variable heavy domain and D3H44 variable light domain plus the D3H44 constant domain, and bound slightly weaker to the chimeric Fab with murine D3 variable light domain and D3H44 variable heavy domain. The authors concluded that the D3H44 variable light domain made more important contributions to the idiotope than the D3H44 variable heavy domain.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |