| identifier: | 1927495 |
| description: |
epitope description:V28, S56, K75, I101, E102, S104, D105, Q119, L121, S145, P147, G148, S149, S150, P151, S152, G165, G166, K167, L187, Q188, N189, Q190, K191
antigen name:T-cell surface glycoprotein CD4
host organism:Mus musculus BALB/c
antibody name:Ibalizumab
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
21134642 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1022159 |
| landingPage: |
http://www.iedb.org/assay/1927495 |
| type: |
Literature
|
| publicationVenue: |
Structure
|
| dates: |
2010
|
| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
Michael M Freeman
Michael S Seaman
Sophia Rits-Volloch
Xinguo Hong
Chia-Ying Kao
David D Ho
Bing Chen
|
| method: |
x-ray crystallography
|
| name: |
Crystal structure of HIV-1 primary receptor CD4 in complex with a potent antiviral antibody.
|
| description: |
Epitope residues are calculated from the structure [PDB: 3O2D] as the antigen residues at 4 Å
distance from the antibody.
The epitope of Ibalizumab Fab on a two-domain fragment of CD4 was determined from the crystal structure of the complex, solved by molecular replacement. There is one Fab-CD4 complex per asymmetric unit.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |