| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1002210 |
| landingPage: |
http://www.iedb.org/assay/1403365 |
| type: |
Literature
|
| publicationVenue: |
Acta Crystallogr D Biol Crystallogr
|
| dates: |
2005
|
| study type: | b cell assays |
| subject species: | Hepatitis C virus |
| fullName: |
René
e Mé
nez
Nicholas G Housden
Stephen Harrison
Colette Jolivet-Reynaud
Michael G Gore
Enrico Adriano Stura
|
| method: |
x-ray crystallography
|
| name: |
Different crystal packing in Fab-protein L semi-disordered peptide complex.
|
| description: |
The minimal recognized epitope is QIVGGVYLL of HCV core (residues 29&ndash
37).
The epitope of 19D9D6 Fab' on the HCV core peptide was determined from the crystal structure of the complex. The complex crystallized in two space groups: The space group of this structure is space group is P21212. In order to make the crystallization possible, use was made of a single immunoglobulin-binding domain of protein L mutant D55A/L57H/Y64W from Peptostreptococcus magnus (PpL), a bacterial protein that can bind the variable region (Fv) of a large population of antibodies through its light chain with no interference with antibody-antigen recognition.The crystal unit contains two complexes of a peptide bound to a antibody: chains P,(B,A) and Q,(D,C), with antibody heavy and light chains shown in parentheses. The epitopes are different in two complexes; therefore, both were curated.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |