| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1001555 |
| landingPage: |
http://www.iedb.org/assay/1812402 |
| type: |
Literature
|
| publicationVenue: |
J Mol Biol
|
| dates: |
2003
|
| study type: | b cell assays |
| subject species: | Streptomyces lividans |
| fullName: |
Yufeng Zhou
Roderick MacKinnon
|
| method: |
x-ray crystallography
|
| name: |
The occupancy of ions in the K+ selectivity filter: charge balance and coupling of ion binding to a protein conformational change underlie high conduction rates.
|
| description: |
The epitope residues are calculated from the PDB structure as the antigen residues at 4 Å
distance from the antibody and are as follows: [PDB: 1R3J] Y45, L49, R52, G53, A54, P55, G56, A57, Q58, I60, T61, Y62, R64 [PDB: 1R3K] Y45, L49, R52, G53, A54, P55, G56, A57, Q58, I60, T61, Y62, P63, R64 [PDB: 1R3I] Y45, L49, A50, R52, G53, A54, P55, G56, A57, Q58, I60, T61, Y62, R64 [PDB: 1R3L] Y45, L49, R52, G53, A54, P55, G56, A57, Q58, I60, T61, Y62, R64
The epitope of Fab on the KcsA potassium channel, in the presence of a high concentration of Rb+, was determined from the crystal structure of the complex. The C-terminal 35 amino acids of KcsA were removed by proteolysis.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |