Immunological Data Discovery Index
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identifier: 1910664
description:
epitope description:S180, N181, S182, Y184, E216, Q242, R243, G244, G245, R246, Q247, T248, E283, S284, H285, N287, L318
antigen name:Integrin alpha-1
host organism:Mus musculus
antibody name:AQC2 mutant (H:T50V/K64E, L:S28Q/N52Y)
aggregation:
instance of dataset
availability:
available
primaryPublications: 16597831
authorizations:
registration not required
accessURL: http://www.iedb.org/reference/1018828
landingPage: http://www.iedb.org/assay/1910664
type:
Literature
publicationVenue:
Protein Sci
dates:
2006
study type: b cell assays
subject species: Homo sapiens
fullName:
Louis A Clark
P Ann Boriack-Sjodin
John Eldredge
Christopher Fitch
Bethany Friedman
Karl J M Hanf
Matthew Jarpe
Stefano F Liparoto
You Li
Alexey Lugovskoy
Stephan Miller
Mia Rushe
Woody Sherman
Kenneth Simon
Herman Van Vlijmen
method:
x-ray crystallography
name:
Affinity enhancement of an in vivo matured therapeutic antibody using structure-based computational design.
description:
Epitope residues are calculated from the structure [PDB: 2B2X] as the antigen residues at 4 Å
distance from the antibody. A chimeric human/rat alpha1ß
1 integrin I domain protein was used that contained the rat sequence, in which four residues that differ between the rat and human sequences were exchanged with the human Integrin counterparts to allow anti-human integrin antibody binding. Three of the four exchanged amino acids are epitope residues, Q218, R219, R222. The other contact residues are conserved between the rat and human sequences except for Y264, which corresponds to H288 in the human sequence.
The epitope of AQC2 quadruple mutant Fab on the I domain of a human/rat chimeric integrin was determined from the crystal structure of the complex. Recombinant chimeric human/rat alpha1ß1 integrin I domain contained the rat sequence, in which four residues that differ between the rat and human sequences were exchanged with the human Integrin counterparts to allow anti-human integrin antibody binding. There are two complexes in the asymmetric unit. Three of the four exchanged amino acids are epitope residues, Q218, R219, R222. The other contact residues are conserved between the rat and human sequences except for, Y264, which corresponds to H288 in the human sequence.

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