|
Domain binding and function: The FHA domain, or Forkhead-Associated domain, was originally identified as a conserved region of forkhead transcription factors. It is 65À100 amino acids long, contains several highly conserved key residues, and is found primarily in eukaryotic nuclear proteins. FHA domainÀcontaining 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), 1169À1182.
Examples of Domain Proteins:
|
 |
| The N-terminal FHA domain of Rad 53p bound to a phospho-threonine peptide (red). | |
