Immunological Data Discovery Index
Immunological Data Discovery Index
| authorizations: |
registration not required
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| accessURL: |
http://www.iedb.org/reference/1027115 |
| landingPage: |
http://www.iedb.org/assay/2021880 |
| type: |
Literature
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| publicationVenue: |
J Biol Chem
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| dates: |
2014
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| study type: | b cell assays |
| subject species: | Clostridioides difficile |
| fullName: |
Tomohiko Murase
Luiz Eugenio
Melissa Schorr
Greg Hussack
Jamshid Tanha
Elena N Kitova
John S Klassen
Kenneth K S Ng
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| method: |
x-ray crystallography
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| name: |
Structural basis for antibody recognition in the receptor-binding domains of toxins A and B from Clostridium difficile.
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| description: |
The epitope residues were calculated from [PDB: 4NBY] as the antigen residues at 4Å
atomic distance from the antibody. Calculated contact residues are I74, P88, A89, N90, T91, Y103, R106, F107, Y109, L110, H111, D112, and R159 in [PDB: 4NC1].
The epitope of A20.1 VHH on the TcdA-A2 RBD fragment (residues 2456-2710) was determined from the crystal structure of the ternary complex of A20.1 and A26.8H6 VHHs bound to TcdA-A2, solved by molecular replacement. There are two molecules each of A20.1 VHH (chains C and D), A26.8H6 VHH (chains E and F) and TcdA-A2 (chains A and B) in the asymmetric unit. The A20.1 VHH binds to epitope 2 near the N-terminal end of TcdA-A2 rather than epitope 1 in the C-terminal part, although binding of A26.8H6 does not appear to sterically hinder binding to epitope 1.
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| name: |
iedb
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| homePage: |
http://www.iedb.org |
