| identifier: | 2019473 |
| description: |
epitope description:S31, S37, G38, Y40, G108, S117, G118, G119, F126, N180, N181, Y183, E186, I187, F188, N189, Q190, S191, Y194, Q234, E235, A238, I239, T240, Q241, D242
antigen name:Methanococcus maripaludis protein
host organism:Mus musculus BALB/c
antibody name:645-2
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
24291792 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1027072 |
| landingPage: |
http://www.iedb.org/assay/2019473 |
| type: |
Literature
|
| publicationVenue: |
Nature
|
| dates: |
2013
|
| study type: | b cell assays |
| subject species: | Methanococcus maripaludis |
| fullName: |
Ioannis Manolaridis
Kiran Kulkarni
Roger B Dodd
Satoshi Ogasawara
Ziguo Zhang
Ganka Bineva
Nicola O' Reilly
Sarah J Hanrahan
Andrew J Thompson
Nora Cronin
So Iwata
David Barford
|
| method: |
biological activity
|
| name: |
Mechanism of farnesylated CAAX protein processing by the intramembrane protease Rce1.
|
| description: |
The epitope residues were calculated from [PDB: 4CAD] as the antigen residues at 4Å
atomic distance from the antibody.
The epitope-specific Fab645-2 does not inhibit the endoprotease activity of MmRce1. The proteolytic activity of MmRce1 on farnesylated peptides was determined by fluorescence resonance energy transfer (FRET) assay.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |