| identifier: | 1975987 |
| description: |
epitope description:A: R43, E44, L47, R48, H50, P51, C52, V53, S54, D55, Q56, E57; B: A49, H50, P51, N78
antigen name:Potassium channel subfamily K member 4
host organism:Mus musculus
antibody name:13E9
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
23341632 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1025554 |
| landingPage: |
http://www.iedb.org/assay/1975987 |
| type: |
Literature
|
| publicationVenue: |
Proc Natl Acad Sci U S A
|
| dates: |
2013
|
| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
Stephen G Brohawn
Ernest B Campbell
Roderick MacKinnon
|
| method: |
x-ray crystallography
|
| name: |
Domain-swapped chain connectivity and gated membrane access in a Fab-mediated crystal of the human TRAAK K+ channel.
|
| description: |
The epitope residues were calculated from [PDB: 4I9W] as the antigen residues at 4 Å
atomic distance from the antibody. The epitope is located on both identical subunits of the channel. There is a mismatch of residue Q104 in PDB and the corresponding residue N78 in the Genbank record, due to introduction of the Q104N mutation to remove the N-linked glycosylation site.
The epitope of 13E9 FAb on TRAAK (TWIK-related arachidonic acid-stimulated K+ channel) was determined from the crystal structure of the complex, solved by molecular replacement. The TRAAK molecule was C-terminally truncated by 119 aa and had two mutations (N104Q/N108Q) to remove N-linked glycosylation sites. The asymmetric unit contains one channel, which consists of two identical subunits arranged with twofold symmetry, and two Fab molecules.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |