| identifier: | 1989487 |
| description: |
epitope description:Y316, R334, T363, K399, E400, E424, I425, R427, R429, K454, E455, S457, K479, L480, F481, G482, T483, S484
antigen name:Epidermal growth factor receptor
host organism:Lama glama
antibody name:Ega1
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
23791944 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1026704 |
| landingPage: |
http://www.iedb.org/assay/1989487 |
| type: |
Literature
|
| publicationVenue: |
Structure
|
| dates: |
2013
|
| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
Karl R Schmitz
Atrish Bagchi
Rob C Roovers
Paul M P van Bergen en Henegouwen
Kathryn M Ferguson
|
| method: |
surface plasmon resonance (SPR)
|
| name: |
Structural evaluation of EGFR inhibition mechanisms for nanobodies/VHH domains.
|
| description: |
The epitope residues were calculated from [PDB: 4KRO] as the antigen residues at 4Å
atomic distance from the antibody.
The affinity of epitope-specific nanobody EgA1 for the soluble EGF Receptor extracellular region was determined by surface plasmon resonance. Nanobody EgA1 bound with similar affinity (KD = 356 nM) to truncated EGFR with most of domain IV deleted (sEGFR501) and to EGFR variant III (EGFRvIII; KD = 822 nM), which lacks domain I and much of domain II. Nanobody EgA1 did not bind to the isolated EGFR domain 3.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |