| identifier: | 1852666 |
| 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/1852666 |
| 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 the EcCLC E148Q mutant transporter was determined from the crystal structure of the complex in the presence of 0 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 |