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identifier: 1852667
description:
epitope description:A: K243, D246, P248, L249, N250, P380, Q381, Y382, H383; B: I231, H234, E235
antigen name:H(+)/Cl(-) exchange transporter ClcA
host organism:Mus musculus
antibody name:10EC3/G4
aggregation:
instance of dataset
availability:
available
primaryPublications: 16341087
authorizations:
registration not required
accessURL: http://www.iedb.org/reference/1019326
landingPage: http://www.iedb.org/assay/1852667
type:
Literature
publicationVenue:
EMBO J
dates:
2006
study type: b cell assays
subject species: Escherichia coli
fullName:
verine Lobet
Raimund Dutzler
method:
x-ray crystallography
name:
Ion-binding properties of the ClC chloride selectivity filter.
description:
The epitope residues are calculated from the PDB structure [PDB: 2EXW] as the antigen residues at 4 Å
distance from the antibody. All three structures give the same epitope.
The epitope of the Fab on theEcCLC S107A/E148Q/Y445A triple mutant transporter was determined from the crystal structure of the complex in the presence of 100 mM Br-, solved by molecular replacement. The EcCLC transporter is a homodimer and bound two Fabs symmetrically. The epitope is located on both subunits but is identical.

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