Phospho-Ser/Thr Binding: FHA Domain
The N-terminal FHA domain of Rad 53p bound to a phospho-threonine peptide (red).
Domain Binding and Function
The FHA domain, or Forkhead-Associated domain, was originally identified as a conserved region of forkhead transcription factors. It is 65–100 amino acids long, contains several highly conserved key residues, and is found primarily in eukaryotic nuclear proteins. FHA domain—containing proteins are also found in certain prokaryotes, such as mycoplasma bacteria. The FHA domain mediates phosphopeptide interactions with proteins phosphorylated by serine/threonine kinases. The first FHA domain of Rad53 binds to a pTXXD motif with a Kd = 1.6 µM, while other FHA domains also bind to pTXXX peptides.
Structure Reference
- Durocher, D. et al. (2000) Mol. Cell 6 (5), 1169–1182.
Examples of Domain Proteins
Binding Examples
| FHA Domain Proteins | Binding Partners |
|---|---|
| KAPP Ser/Thr Phosphatase | pRLK5 (phosphorylated) Arabidopsis receptor-like Ser/Thr Kinase |
| Rad53 S. cerevisiae Ser/Thr Kinase | pRad9 (phosphorylated) S. cerevisiae checkpoint control protein |
