| identifier: | 1974416 |
| description: |
epitope description:S158, G159, S160, E194, E195, F196, R197, L221, L222, G223, R224, T225, G259, E260, F262, G263, A290
antigen name:Integrin alpha-M
host organism:Mus musculus BALB/c
antibody name:107
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
22095715 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1024799 |
| landingPage: |
http://www.iedb.org/assay/1974416 |
| type: |
Literature
|
| publicationVenue: |
J Immunol
|
| dates: |
2011
|
| study type: | b cell assays |
| subject species: | Homo sapiens |
| fullName: |
Bhuvaneshwari Mahalingam
Kaouther Ajroud
José
Luis Alonso
Saurabh Anand
Brian D Adair
Alberto L Horenstein
Fabio Malavasi
Jian-Ping Xiong
M Amin Arnaout
|
| method: |
biological activity
|
| name: |
Stable coordination of the inhibitory Ca2+ ion at the metal ion-dependent adhesion site in integrin CD11b/CD18 by an antibody-derived ligand aspartate: implications for integrin regulation and structure-based drug design.
|
| description: |
The epitope residues were calculated from [PDB: 3Q3G] as the antigen residues at 4 Å
atomic distance from the antibody. [PDB: 3QA3] gives identical epitopes.
The epitope-specific Fab 107 did not exhibit agonist-like activity upon binding low affinity human CD11b/CD18 integrin stably expressed on K562 cells, as measured by the binding of activation reporter mAb 24 to detect a conformational switch from the low- to high-affinity state in the CD11b A domain. Fab 107 prevented the conformational switch of CD11bA to the high-affinity state in agonist-preactivated integrin on human neutrophils.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |