| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1026659 |
| landingPage: |
http://www.iedb.org/assay/1989311 |
| type: |
Literature
|
| publicationVenue: |
Biochim Biophys Acta
|
| dates: |
2013
|
| study type: | b cell assays |
| subject species: | Escherichia coli K-12 |
| fullName: |
David Oyen
Rainer Wechselberger
Vasundara Srinivasan
Jan Steyaert
John N Barlow
|
| method: |
nuclear magnetic resonance (NMR)
|
| name: |
Mechanistic analysis of allosteric and non-allosteric effects arising from nanobody binding to two epitopes of the dihydrofolate reductase of Escherichia coli.
|
| description: |
The epitope region on DHFR:folate bound by epitope-specific nanobody Nb113 on DHFR:folate was mapped by chemical shift perturbation NMR. Nanobody Nb113 bound to a region distal to the NADPH and substrate binding sites and therefore represents an allosteric site.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |