| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1024749 |
| landingPage: |
http://www.iedb.org/assay/1965352 |
| type: |
Literature
|
| publicationVenue: |
Proc Natl Acad Sci U S A
|
| dates: |
2011
|
| study type: | b cell assays |
| subject species: | Streptomyces lividans |
| fullName: |
Serdar Uysal
Luis G Cuello
D Marien Cortes
Shohei Koide
Anthony A Kossiakoff
Eduardo Perozo
|
| method: |
x-ray crystallography
|
| name: |
Mechanism of activation gating in the full-length KcsA K+ channel.
|
| description: |
The epitope is located on two monomers of the antigen tetramer. The epitope residues were calculated from the PDB structure as the antigen residues at 4 Å
distance from the antibody.
The epitope of Fab2 on full-length voltage-gated potassium channel (KcsA) in its open conformation was determined from the crystal structure of the complex, solved by molecular replacement. The complex contains two Fab2 molecules bound to KcsA tetramer. Full-length KcsA in the constitutively open conformation was stabilized through mutations at the pH sensor (OM-FL-KcsA).
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |