Hydrogen bonding and solvent structure in an antigen-antibody interface. Crystal structures and thermodynamic characterization of three Fv mutants complexed with lysozyme.

Title:

Hydrogen bonding and solvent structure in an antigen-antibody interface. Crystal structures and thermodynamic characterization of three Fv mutants complexed with lysozyme.

Dataset

identifier:	1771931
description:	epitope description:D36, N37, G40, Y41, S42, N45, G120, K134, G135, T136, D137, V138, Q139, I142, R143 antigen name:Gal d 4 host organism:Mus musculus BALB/c antibody name:D1.3 mutant VH Y101F
aggregation:	instance of dataset
availability:	available
primaryPublications:	8952503

Access

authorizations:	registration not required
accessURL:	http://www.iedb.org/reference/1019320
landingPage:	http://www.iedb.org/assay/1771931

Publication

type:	Literature
publicationVenue:	Biochemistry
dates:	1996

Dimension

study type:	b cell assays
subject species:	Gallus gallus

Person

fullName:	B A Fields F A Goldbaum W Dall'Acqua E L Malchiodi A Cauerhff F P Schwarz X Ysern R J Poljak R A Mariuzza

Data Type

method:	calorimetry

Study

name:	Hydrogen bonding and solvent structure in an antigen-antibody interface. Crystal structures and thermodynamic characterization of three Fv mutants complexed with lysozyme.
description:	Epitope specific Fv D1.3 mutant VH Y101F bound to lysozyme (HEL) with a binding constant of 4.0 x 10⁶ M-1. This was 70-fold lower than that of wild type D1.3 complexed with HEL (2.7 x 10⁸ M-1).

Data Repository

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

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