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identifier: 1989486
description:
epitope description:K346, D347, L349, H370, L372, P373, V374, R377, D379, F381, T382, Q408, H433, S442
antigen name:Epidermal growth factor receptor
host organism:Lama glama
antibody name:7D12
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/1989486
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: 4KRL] (pH 6.0) as the antigen residues at 4Å
atomic distance from the antibody and are the following: L325, H346, L348, P349, V350, R353, D355, F357, T358, Q384, H409, S418. From [PDB: 4KRM] (pH 3.5), the epitope residues are: K322, D323, L325, L348, P349, V350, R353, D355, F357, T358, Q384, S418. Here, the combined epitope is provided.
The affinity of epitope-specific nanobody 7D12 for domain 3 of the EGF Receptor extracellular region was determined by surface plasmon resonance. Nanobody 7D12 bound with higher affinity to domain 3 than to the entire EGFR extracellular region (KD = 219 nM).

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