Immunological Data Discovery Index
Immunological Data Discovery Index
| identifier: | 1511684 |
| description: |
epitope description:L237, G238, G239, K257, A260, K261, T264, W269, S270, G271, E272, K273, Y276, N279, G283, W284, G285, G308, G309, S310, S311, G413
antigen name:Pancreatic alpha-amylase
host organism:Camelus dromedarius
antibody name:AMB7
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| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
11960990 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1001546 |
| landingPage: |
http://www.iedb.org/assay/1511684 |
| type: |
Literature
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| publicationVenue: |
J Biol Chem
|
| dates: |
2002
|
| study type: | b cell assays |
| subject species: | Sus scrofa |
| fullName: |
Aline Desmyter
Silvia Spinelli
Francoise Payan
Marc Lauwereys
Lode Wyns
Serge Muyldermans
Christian Cambillau
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| method: |
x-ray crystallography
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| name: |
Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology.
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| description: |
The epitope residues were calculated as the antigen residues interacting with the antibody at 4 Å
atomic distance based on the structure [PDB: 1KXT].
The epitope of AMB7 VHH on porcine pancreatic alpha-amylase was determined from the crystal structure of the complex, solved by molecular replacement. AMB7 VHH binds the antigen outside the catalytic site and inhibits only partially the amylase activity. The crystal contains three complexes in the asymmetric unit.
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| name: |
iedb
|
| homePage: |
http://www.iedb.org |
