| identifier: | 2119469 |
| description: |
epitope description:A: N24, P27, V29, T155, K156, E159, L161, Y190, T192, V194, T195, N196, I199; B: L170, K171, V172
antigen name:Glutamate-gated chloride channel alpha
host organism:Mus musculus
antibody name:anti-GluCl
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
25143115 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1028145 |
| landingPage: |
http://www.iedb.org/assay/2119469 |
| type: |
Literature
|
| publicationVenue: |
Nature
|
| dates: |
2014
|
| study type: | b cell assays |
| subject species: | Caenorhabditis elegans |
| fullName: |
Thorsten Althoff
Ryan E Hibbs
Surajit Banerjee
Eric Gouaux
|
| method: |
x-ray crystallography
|
| name: |
X-ray structures of GluCl in apo states reveal a gating mechanism of Cys-loop receptors.
|
| description: |
The epitope is located on two monomers of the homopentamer. Epitope residues are calculated from the structures [PDB: 4TNW and 4TNV] as the antigen residues at 4 Å
distance from the antibody. The combined epitope is provided. Contact residues G25, G26, T189, and S193 are present only in PDB: 4TNV] and T195 is present only in [PDB: 4TNW].
The epitope of the Fab on GluCl in the presence of POPC (1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine) was determined from the crystal structure of the complex, solved by molecular replacement. The GluCl construct had tuncated N- and C-termini, and residues K345-K402 in the mature sequence, corresponding to the M3-M4 loop, were substituted with residues AGT. The GluCl-Fab complex forms a pinwheel shape comprising a cylindrical homopentamer of GluC subunits with Fab molecules bound at each subunit interface. The epitope is located on two monomers of the homopentamer.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |