| identifier: | 1667738 |
| 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:anti-ClC Fab
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
12649487 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1001548 |
| landingPage: |
http://www.iedb.org/assay/1667738 |
| type: |
Literature
|
| publicationVenue: |
Science
|
| dates: |
2003
|
| study type: | b cell assays |
| subject species: | Escherichia coli K-12 |
| fullName: |
Raimund Dutzler
Ernest B Campbell
Roderick MacKinnon
|
| method: |
x-ray crystallography
|
| name: |
Gating the selectivity filter in ClC chloride channels.
|
| description: |
The epitope residues are calculated based on the Fab-antigen complex structures [PDB: 1OTS, 1OTT, 1OTU] as the protein antigen residues consisting of at least one atom separated from any antibody atom at or less than 4 Å
distance. The epitope is located on both polypeptide chains of the antigen homodimer.
The epitope of the anti-ClC Fab on a ClC homodimer containing the E148Q mutation was determined from the crystal structure of the complex. The mutation is not involved in the epitope. The structure contains two Fab molecules (chains C,D and E,F) each bound to one of two subunits of the homodimeric channel (chains A,B). Each identical subunit forms its own independent pore for Cl- ions. According to calculations, the epitopes for two Fabs are identical, therefore, only one complex is curated here.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |