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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.

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