| Title: | A mutational analysis of binding interactions in an antigen-antibody protein-protein complex. |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1019573 |
| landingPage: |
http://www.iedb.org/assay/1769500 |
| type: |
Literature
|
| publicationVenue: |
Biochemistry
|
| dates: |
1998
|
| study type: | b cell assays |
| subject species: | Gallus gallus |
| fullName: |
W Dall'Acqua
E R Goldman
W Lin
C
D Tsuchiya
H Li
X Ysern
B C Braden
Y Li
S J Smith-Gill
R A Mariuzza
|
| method: |
surface plasmon resonance (SPR)
|
| name: |
A mutational analysis of binding interactions in an antigen-antibody protein-protein complex.
|
| description: |
The epitope residues were calculated based on the 4 Å
atomic distance between the antigen and the antibody from [PDB: 1A2Y].
Epitope specific scFv D1.3 bound to hen egg white lysozyme (HEL). Binding to mutants of HEL with alanine substitutions at 12 of 13 total non-glycine residues in contact with D1.3 showed that substitutions at four positions significantly decreased binding. The mutants and apparent KA were: Q121A, KA = 6.2 x 105M^-1; R125A, KA = 3.6 x 106M^-1; I124A, KA = 1 x 107M^-1; and D119A, KA = 1.6 x 107M^-1. The authors conclude that only a small subset of the contact residues account for a large portion of the binding energy.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |