Immunological Data Discovery Index
Immunological Data Discovery Index
| identifier: | 1708384 |
| description: |
epitope description:F89, Y90, L91, E92, E93, V94, M95, P96, Q97, A98, E99, N100, Q101, K143, N144, A145, F146, N147, K148, L149, Q150, E151, K152, G153, I154, Y155
antigen name:Interleukin-10
host organism:Rattus norvegicus
antibody name:9D7
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
12121653 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/335 |
| landingPage: |
http://www.iedb.org/assay/1708384 |
| type: |
Literature
|
| publicationVenue: |
Structure
|
| dates: |
2002
|
| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
Kristopher Josephson
Brandi C Jones
Leigh J Walter
Ruth DiGiacomo
Stephen R Indelicato
Mark R Walter
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| method: |
biological activity
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| name: |
Noncompetitive antibody neutralization of IL-10 revealed by protein engineering and x-ray crystallography.
|
| description: |
The epitope-specific 9D7 Fab inhibited the binding of IL-10M1 to the receptor IL-10R1, as measured by isothermal calorimetry titration. Fab 9D7 and IL-10R1 bind distinct nonoverlapping sites on IL-10, and the authors show that its neutralization is due to an allosteric mechanism, where the Fab induces conformational changes that indirectly disrupt the IL-10R1 binding site. The antigen IL-10M1 is the “unswapped” monomer of IL-10 and was created by inserting six residues (GGGSGG) between Asn134 and Lys135 of the IL-10 DE loop.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |
