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identifier: 1974406
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/1974406
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:
x-ray crystallography
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 of Fab 107 on the high affinity (open) form of the (Ile316Gly)CD11b A domain was determined from the crystal structure of the complex. The Ile316Gly mutation generates a constitutively active integrin. Each of the four molecules in the asymmetric unit of the complex contains a Ca2+ ion in the metal ion-dependent adhesion site (MIDAS), stabilized by Asp 107 from the Fab 107 heavy chain variable region.

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