| 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: |
Sé
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.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |