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identifier: 1511686
description:
epitope description:Y2, P154, Y155, W203, P204, G205, D206, K208, K243, S245, E246, F248, G249, E282, G285, P288, R291
antigen name:Pancreatic alpha-amylase
host organism:Camelus dromedarius
antibody name:AMD10
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/1511686
type:
Literature
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
method:
x-ray crystallography
name:
Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology.
description:
The epitope residues were calculated as the antigen residues interacting with the antibody at 4 Å
atomic distance based on the structure [PDB: 1KXV].
The epitope of AMD10 VHH on porcine pancreatic alpha-amylase was determined from the crystal structure of the complex, solved by molecular replacement. AMD10 VHH binds the antigen outside the catalytic site and does not inhibit or inhibits only partially its amylase activity. The crystal contains two complexes in the asymmetric unit.

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