| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1019658 |
| landingPage: |
http://www.iedb.org/assay/1903119 |
| type: |
Literature
|
| publicationVenue: |
Proc Natl Acad Sci U S A
|
| dates: |
2009
|
| study type: | b cell assays |
| subject species: |
| fullName: |
Erik W Debler
Roger Mü
ller
Donald Hilvert
Ian A Wilson
|
| method: |
x-ray crystallography
|
| name: |
An aspartate and a water molecule mediate efficient acid-base catalysis in a tailored antibody pocket.
|
| description: |
The crystal structure of catalytic antibody Fab 13G5 Glu(L34)Gln in complex with the epitope was determined by molecular replacement. Position 34 of the antibody light chain is in the active site, but does not directly interact with bound ligand and is not essential. The ionization state of the residue nevertheless affects antibody activity. Antibody mutant 13G5 Glu(L34)Gln has a broader pH optimum for the elimination reaction.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |