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identifier: 1713586
description:
epitope description:E604, D620, K627, D630
antigen name:Thyroid peroxidase (UniProt:P07202)
host organism:Homo sapiens
antibody name:126TP5, 126TP14
aggregation:
instance of dataset
availability:
available
primaryPublications: 16959834
authorizations:
registration not required
accessURL: http://www.iedb.org/reference/1017349
landingPage: http://www.iedb.org/assay/1713586
type:
Literature
publicationVenue:
Endocrinology
dates:
2006
study type: b cell assays
subject species: Homo sapiens
fullName:
Marlena Dubska
J Paul Banga
Danuta Plochocka
Grazyna Hoser
E Helen Kemp
Brian J Sutton
Andrzej Gardas
Monika Gora
method:
flow cytometry
name:
Structural insights into autoreactive determinants in thyroid peroxidase composed of discontinuous and multiple key contact amino acid residues contributing to epitopes recognized by patients' autoantibodies.
description:
Human monoclonal Fab fragments (rhFabs) specific for the immunodominant region B (IDR-B) bound to wild-type TPO and selected point mutants by FACS. A combination of four mutations K627G/E604A/D620R/D624S reduced binding approximately 6-fold and a combination of five mutations K627G/E604A/D620R/D624S/D630N abolished binding, although the single mutations did not affect binding. The results were confirmed by ELISA, which showed greater sensitivity to the mutations with single mutations K627G, E604A, D630N and D620R showing significantly reduced binding. The authors conclude that residues K627, E604, D620, D624, and D630 contribute to the IDR-B epitope.

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