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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.

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