Immunological Data Discovery Index
Immunological Data Discovery Index
| Title: | Evaluation of mutagenesis for epitope mapping. Structure of an antibody-protein antigen complex. |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1010412 |
| landingPage: |
http://www.iedb.org/assay/1513458 |
| type: |
Literature
|
| publicationVenue: |
J Biol Chem
|
| dates: |
1993
|
| study type: | b cell assays |
| subject species: | Escherichia coli |
| fullName: |
L Prasad
S Sharma
M Vandonselaar
J W Quail
J S Lee
E B Waygood
K S Wilson
Z Dauter
L T Delbaere
|
| method: |
x-ray crystallography
|
| name: |
Evaluation of mutagenesis for epitope mapping. Structure of an antibody-protein antigen complex.
|
| description: |
The crystal structure of the Jel42 Fab fragment bound to E. coli phosphocarrier protein HPr was solved to 2.8 angstroms. Nine of the 14 contact residues (M1, F2, Q3, Q4, S41, S64, E66, E70, Q71, and E75) were correctly assigned by mutagenesis studies. Contact residues that were not assigned by site-directed mutagenesis were due to lack of mutants generated (Met-1 and Gly-67) or the ability of the residue to be substituted and retain binding (Glu-68 and Lys-72) or other interpretations (Thr-34). Other residues incorrectly assigned to the epitope by mutagenesis (Glu-5, Ser-31, Asp-69, and His-76) are just outside the periphery of the epitope. Mutations in these residues reduced binding by < 10-fold.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |