Article
Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis.
The EMBO journal - 7 Feb 2007
Ottmann Christian, Yasmin Lubna, Weyand Michael, Veesenmeyer Jeffrey L, Diaz Maureen H, Palmer Ruth H, Francis Matthew S, Hauser Alan R, Wittinghofer Alfred, Hallberg Bengt
Abstract excerpt
14-3-3 proteins are phosphoserine/phosphothreonine-recognizing adapter proteins that regulate the activity of a vast array of targets. There are also examples of 14-3-3 proteins binding their targets via unphosphorylated motifs. Here we present a structural and biological investigation of the phosphorylation-independent interaction between 14-3-3 and exoenzyme S (ExoS), an ADP-ribosyltransferase toxin of...
Topics
- 14-3-3 Proteins
- ADP Ribose Transferases
- Animals
- Bacterial Toxins
- Blotting, Western
- Crystallography
- DNA Primers
- Female
- HeLa Cells
- Humans
- Mice
- Mice, Inbred BALB C
- Models, Molecular