| identifier: | 2015845 |
| description: |
epitope description:A: S152, N153, W169, G174, S175, S202, T203, Q205, E206, T208, S209, G241, L242; C: T142, T144, P178, V179, N181
antigen name:Hemagglutinin
host organism:Mus musculus BALB/c
antibody name:HC63
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
11886266 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1032 |
| landingPage: |
http://www.iedb.org/assay/2015845 |
| type: |
Literature
|
| publicationVenue: |
Virology
|
| dates: |
2002
|
| study type: | b cell assays |
| subject species: | Influenza A virus |
| fullName: |
C Barbey-Martin
B Gigant
T Bizebard
L J Calder
S A Wharton
J J Skehel
M Knossow
|
| method: |
x-ray crystallography
|
| name: |
An antibody that prevents the hemagglutinin low pH fusogenic transition.
|
| description: |
The epitope is located on HA1 chains of two monomers, with 5 residues (T142, T144, P178, V179, N181) bound in one monomer and 13 residues (S152, N153, W169, G174, S175, S202, T203, Q205, E206, S209, T208, G241, L242) bound in another. The epitope overlaps the sialic acid receptor-binding site.
The crystal structure of HC63 Fab bound to X-31 BHA complex was solved by molecular replacement. Antibody name and chain isotypes are specified in the paper [PMID: 10944356]. The BHA fragment is composed of the complete mature HA1 and the extracellular domain of HA2. There are two Fab molecules and a trimer of HA1/HA2 chains in the asymmetric unit. HA-binding sites of both Fabs, the first (chains H and L) and the second (chains T and U) are identical and located on HA1 chains A and C for the first Fab, and C and E for the second Fab of two monomers. A third potential Fab binding site on the HA1 chains E and A is free.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |