| identifier: | 1977831 |
| description: |
epitope description:L121, T280, N281, N282, A283, K284, S365, G366, G367, D368, E370, I371, N419, W421, G423, G425, Q426, T449, R450, D451, G452, G453, A454, N456, R463, G467, N468, K470, R474
antigen name:Envelope glycoprotein gp160
host organism:Homo sapiens
antibody name:12A21
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
23540694 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1025766 |
| landingPage: |
http://www.iedb.org/assay/1977831 |
| type: |
Literature
|
| publicationVenue: |
Cell
|
| dates: |
2013
|
| study type: | b cell assays |
| subject species: | Human immunodeficiency virus 1 |
| fullName: |
Florian Klein
Ron Diskin
Johannes F Scheid
Christian Gaebler
Hugo Mouquet
Ivelin S Georgiev
Marie Pancera
Tongqing Zhou
Reha-Baris Incesu
Brooks Zhongzheng Fu
Priyanthi N P Gnanapragasam
Thiago Y Oliveira
Michael S Seaman
Peter D Kwong
Pamela J Bjorkman
Michel C Nussenzweig
|
| method: |
x-ray crystallography
|
| name: |
Somatic mutations of the immunoglobulin framework are generally required for broad and potent HIV-1 neutralization.
|
| description: |
The epitope residues were calculated from [PDB: 4JPW] as the antigen residues at 4 Å
atomic distance from the antibody. Additional contact residue G124 is a replacement residue for a deleted loop.
The epitope of broadly and potently neutralizing antibody Fab 12A21 on HIV-1 gp120 core from clade A/E 73TH057 (with mutation H375S) was determined from the crystal structure of the complex.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |