| identifier: | 1708357 |
| description: |
epitope description:V: F43; W: Y71, K74, Q105, I106, M107, R108, I109, H112, Q113, G114, Q115, H116, I117, G118, E119, M120
antigen name:Vascular endothelial growth factor A (UniProt:P15692)
host organism:Mus musculus BALB/c
antibody name:Fab-12 variant Y0317
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| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
10543973 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/312 |
| landingPage: |
http://www.iedb.org/assay/1708357 |
| type: |
Literature
|
| publicationVenue: |
J Mol Biol
|
| dates: |
1999
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| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
Y Chen
C Wiesmann
G Fuh
B Li
H W Christinger
P McKay
A M de Vos
H B Lowman
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| method: |
radio immuno assay (RIA)
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| name: |
Selection and analysis of an optimized anti-VEGF antibody: crystal structure of an affinity-matured Fab in complex with antigen.
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| description: |
The epitope residues were calculated from [PDB: 1CZ8] as the antigen residues at 4Å
atomic distance from the antibody. The epitope is located on both chains of a VEGF homodimer.
The in vitro affinity-matured anti-VEGF monoclonal antibody (Y0317, IgG form) shows stronger binding to the epitope and a different fine specificity compared with the humanized parental anti-VEGF monoclonal antibody (Fab12, IgG form). The residues that profoundly decrease binding of Fab12 (IgG form) to VEGF are shown to be M81, R82, I83 and G92 by alanine scanning analysis by ELISA at 37ºC, whereas only residues M81 and G92 are critical for Y0317 (IgG form) binding. In fact, the Kd of the Y0317 Fab is 19.8 ± 4.3 pM compared with 433 ± 116 pM for Fab12 (in a radiolabelled VEGF binding assay at 23 °C).
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| name: |
iedb
|
| homePage: |
http://www.iedb.org |