| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1014161 |
| landingPage: |
http://www.iedb.org/assay/1630832 |
| type: |
Literature
|
| publicationVenue: |
Protein Sci
|
| dates: |
2008
|
| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
Terukazu Nogi
Takeshi Sangawa
Sanae Tabata
Masamichi Nagae
Keiko Tamura-Kawakami
Ayako Beppu
Mitsuharu Hattori
Norihisa Yasui
Junichi Takagi
|
| method: |
x-ray crystallography
|
| name: |
Novel affinity tag system using structurally defined antibody-tag interaction: application to single-step protein purification.
|
| description: |
The structure of the epitope bound by P20.1 Fab was determined by molecular replacement. There are two molecules in the crystallographic asymmetric unit. PDB chains for each complex are: Complex I : Antibody heavy-chain: H, Antibody light-chain: L, epitope chain: P. Complex II : Antibody heavy-chain: I, Antibody light-chain: M, epitope chain: Q. The conformation of the interface residues was almost identical in the two complexes, with minor differences at the periphery. The side chain of H: R53; bends toward the P7 in one of the complexes, acting like a ""lid"". Whereas, in the other complex, it assumes a different conformer, but it still contacts the peptide using its Cbeta.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |