| identifier: | 2019271 |
| description: |
epitope description:A198, I199, N200, A201, P202, A203, N204, I205, Q206, Q207, F208, E209, H210, I211, V212, Q213, L214, R215, P309, N310, A311, Q312, P313, F314, E315, H316, H317
antigen name:Intermediate capsid protein VP6
host organism:Homo sapiens
antibody name:RV6-25
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
24155406 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1027064 |
| landingPage: |
http://www.iedb.org/assay/2019271 |
| type: |
Literature
|
| publicationVenue: |
J Virol
|
| dates: |
2014
|
| study type: | b cell assays |
| subject species: | Rhesus rotavirus |
| fullName: |
Mohammed S Aiyegbo
Ilyas M Eli
Benjamin W Spiller
Dewight R Williams
Robert Kim
David E Lee
Tong Liu
Sheng Li
Phoebe L Stewart
James E Crowe Jr
|
| method: |
electron microscopy
|
| name: |
Differential accessibility of a rotavirus VP6 epitope in trimers comprising type I, II, or III channels as revealed by binding of a human rotavirus VP6-specific antibody.
|
| description: |
The epitope-specific monoclonal antibody RV6-25 was shown to bind double-layer particles (DLPs) using cryo-electron microscopy. The reconstruction of the Fab-DLP complex was computed from 1,062 complex particle images extracted from corresponding cryo-EM micrographs. The estimated final resolution of the RV6-25–DLP complex was 21.5 Å, using the 0.5 FSC criterion.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |