| identifier: | 1557448 |
| description: |
epitope description:V: F43, Y47; W: Y71, K74, Q105, I106, M107, R108, I109, K110, 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 Y0192 (humanized mAb A4.6.1)
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
9753694 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/311 |
| landingPage: |
http://www.iedb.org/assay/1557448 |
| type: |
Literature
|
| publicationVenue: |
Structure
|
| dates: |
1998
|
| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
Y A Muller
Y Chen
H W Christinger
B Li
B C Cunningham
H B Lowman
A M de Vos
|
| method: |
antigen inhibition (~ IC50)
|
| name: |
VEGF and the Fab fragment of a humanized neutralizing antibody: crystal structure of the complex at 2.4 A resolution and mutational analysis of the interface.
|
| description: |
The epitope is composed of residues located in both chains of the VEGF homodimer.
Critical residues for binding of the epitope-specific mAb were determined by alanine scanning. IC50 values for the wild type were compared to mutants of the VEGF binding domain epitope residues. Residues M107, R108, I109, G114, Q115, and G118 showed 22- to 107-fold decreases in affinity relative to the wild type. Smaller, but significant, decreases in binding of about 5–8 fold were found for mutations at positions K74, Q105, K110, E119 and M120.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |