| identifier: | 1838812 |
| description: |
epitope description:H90, D113, Y116, P117, F118, T119, D121, R124, V136, V285, A327, V328, K331, E334, E335, M347, A350, Q351, G353, E354, I355, M356, P357, N358
antigen name:Maltose-binding periplasmic protein
host organism:Homo sapiens
antibody name:sAB MCS2
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
21378967 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1022188 |
| landingPage: |
http://www.iedb.org/assay/1838812 |
| type: |
Literature
|
| publicationVenue: |
Nat Struct Mol Biol
|
| dates: |
2011
|
| study type: | b cell assays |
| subject species: | Escherichia coli |
| fullName: |
Shahir S Rizk
Marcin Paduch
John H Heithaus
Erica M Duguid
Andrew Sandstrom
Anthony A Kossiakoff
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| method: |
x-ray crystallography
|
| name: |
Allosteric control of ligand-binding affinity using engineered conformation-specific effector proteins.
|
| description: |
The epitope residues are calculated form the PDB structure [PDB: 3PGF] as the antigen residues at 4 Å
distance from the antibody.
The epitope of sAB MCS2 on MBP bound to maltose was determined from the crystal structure, solved by molecular replacement. MBP was expressed with a His10 tag followed by a Flag tag at the N-terminus of MBP lacking its periplasmic signal sequence. In contrast to the MBP–MCS2 complex reported here, a previous structure of a sAB based on a monobody scaffold generated without maltose shows that the monobody interacts with an open form of MBP at the maltose-binding site [PDB: 3CSG].
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |