The structure of the anti-c-myc antibody 9E10 Fab fragment/epitope peptide complex reveals a novel binding mode dominated by the heavy chain hypervariable loops.

Title:

The structure of the anti-c-myc antibody 9E10 Fab fragment/epitope peptide complex reveals a novel binding mode dominated by the heavy chain hypervariable loops.

Dataset

identifier:	1835849
description:	epitope description:EQKLISEEDLN host organism:Mus musculus BALB/c antibody name:9E10
aggregation:	instance of dataset
availability:	available
primaryPublications:	18473392

Access

authorizations:	registration not required
accessURL:	http://www.iedb.org/reference/1013847
landingPage:	http://www.iedb.org/assay/1835849

Publication

type:	Literature
publicationVenue:	Proteins
dates:	2008

Dimension

study type:	b cell assays
subject species:

Person

fullName:	Norbert Krauss Helga Wessner Karin Welfle Heinz Welfle Christa Scholz Martina Seifert Kristina Zubow Jacqueline Aÿ Michael Hahn Patrick Scheerer Arne Skerra Wolfgang Hö hne

Data Type

method:	calorimetry

Study

name:	The structure of the anti-c-myc antibody 9E10 Fab fragment/epitope peptide complex reveals a novel binding mode dominated by the heavy chain hypervariable loops.
description:	The epitope is an analog of c-myc proto-oncogene protein, with the mutation: L41->N41. The binding affinity of Fab 9E10 to the epitope was determined by isothermal titration calorimetry. The value in phosphate buffer at 25ºC is shown.

Data Repository

name:	iedb
homePage:	http://www.iedb.org

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