Crystal structure of an in vitro affinity- and specificity-matured anti-testosterone Fab in complex with testosterone. Improved affinity results from small structural changes within the variable domains.

Title:

Dataset

identifier:	1717194
description:	epitope description:testosterone host organism:Mus musculus antibody name:mutant 77
aggregation:	instance of dataset
availability:	available
primaryPublications:	12196551

Access

authorizations:	registration not required
accessURL:	http://www.iedb.org/reference/1017034
landingPage:	http://www.iedb.org/assay/1717194

Publication

type:	Literature
publicationVenue:	J Biol Chem
dates:	2002

Dimension

study type:	b cell assays
subject species:

Person

fullName:	Jarkko Valjakka Ari Hemminki Seija Niemi Hans Sö derlund Kristiina Takkinen Juha Rouvinen

Data Type

method:	surface plasmon resonance (SPR)

Study

name:	Crystal structure of an in vitro affinity- and specificity-matured anti-testosterone Fab in complex with testosterone. Improved affinity results from small structural changes within the variable domains.
description:	Mutant 77 Fab bound to immobilized testosterone-3-carboxymethyloxime-BSA as determined by BIAcore. Mutant 77 Fab has an approximate 15-fold slower dissociation rate and a 40-fold increase in affinity compared to the parent mAb 3-C4F5. Mutant 77 Fab bound specifically to testosterone with minimal cross-reactivity to DHEAS, 5alpha-dihydrotestosterone , or androstenedione.

Data Repository

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

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