| identifier: | 1959744 |
| description: |
epitope description:L32, F33, W36, K64, Y65, Y84, P86, W87, R108, P110, R111, G112, Q113, W115, R116, A118, Q122
antigen name:Glucagon receptor
host organism:Mus musculus Xenomouse
antibody name:mAb1
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
22908259 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1025185 |
| landingPage: |
http://www.iedb.org/assay/1959744 |
| type: |
Literature
|
| publicationVenue: |
Proc Natl Acad Sci U S A
|
| dates: |
2012
|
| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
Christopher M Koth
Jeremy M Murray
Susmith Mukund
Azadeh Madjidi
Alexandra Minn
Holly J Clarke
Terence Wong
Vicki Chiang
Elizabeth Luis
Alberto Estevez
Jesus Rondon
Yingnan Zhang
Isidro Hö
tzel
Bernard B Allan
|
| method: |
x-ray crystallography
|
| name: |
Molecular basis for negative regulation of the glucagon receptor.
|
| description: |
The epitope of mAb1 Fab on the large extracellular domain (ECD) of the glucagon receptor (GCGR) was determined from the crystal structure of the complex, solved by molecular replacement. Alanine scanning mutagenesis experiments across the entire ECD confirmed that Y65, R111, and Q113 are critical residues for mAb1. Mutations Y65A, R111A, or Q113A prevent mAb1 from inhibiting glucagon-induced GCGR activation. NOTE: The mode of interaction described in the paper and that shown in the PDB structure are significantly different.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |