| identifier: | 2007713 |
| description: |
epitope description:D116, P119, D150, R151, A152, T153, N155, R156, R157, T158, D161, G162, I164, Q166, K208
antigen name:Granzyme K
host organism:Mus musculus A/J
antibody name:AFD
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
22362762 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1024620 |
| landingPage: |
http://www.iedb.org/assay/2007713 |
| type: |
Literature
|
| publicationVenue: |
J Biol Chem
|
| dates: |
2012
|
| study type: | b cell assays |
| subject species: | Macaca fascicularis |
| fullName: |
Kenneth J Katschke Jr
Ping Wu
Rajkumar Ganesan
Robert F Kelley
Mary A Mathieu
Philip E Hass
Jeremy Murray
Daniel Kirchhofer
Christian Wiesmann
Menno van Lookeren Campagne
|
| method: |
x-ray crystallography
|
| name: |
Inhibiting alternative pathway complement activation by targeting the factor D exosite.
|
| description: |
The epitope residues were calculated from [PDB: 4D9Q] as the antigen residues at 4Å
atomic distance from the antibody.
The epitope of AFD Fab on cynomolgus Factor D was determined from the crystal structure of the complex. ""There are nine residue differences between human and cynomolgus FD, all of which, with one exception, are located in regions that are distant from the AFD-binding interface. Residue 178 is the exception, with the Glu-178 side chain of human FD engaged in a weak hydrogen bond interaction with HC Thr-28. In comparison, Gln-178 of cynomolgus FD is engaged in a hydrogen bond interaction with HC Asn-31."" In addition, epitope residue A143 is Glu in cynomolgus Factor D. There are two complexes in the asymmetric unit.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |