| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1015107 |
| landingPage: |
http://www.iedb.org/assay/1658277 |
| type: |
Literature
|
| publicationVenue: |
Science
|
| dates: |
2009
|
| study type: | b cell assays |
| subject species: | Rhesus rotavirus |
| fullName: |
Scott T Aoki
Ethan C Settembre
Shane D Trask
Harry B Greenberg
Stephen C Harrison
Philip R Dormitzer
|
| method: |
x-ray crystallography
|
| name: |
Structure of rotavirus outer-layer protein VP7 bound with a neutralizing Fab.
|
| description: |
The epitope residues were calculated based on the PDB structure [PDB: 3FMG] as the antigen residues interacting with the antibody at 4 Å
atomic distance. This epitope is located on one subunit of the antigen, which is a trimer. This epitope is a part of the larger epitope located on two subunits of the antigen trimer.
The epitope-specific mAb 4F8 binds only Ca2+ bound, trimeric VP7. Three Fab fragments bind each trimer. The asymmetric unit contains one monomer (subunit) of VP7 and one Fab molecule. The Fab binds across the outer surface of the inter-subunit contact. Therefore, the whole epitope is located on two subunits, meaning that the epitope derived from the PDB structure is a partial epitope.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |