Hsp90 is a molecular chaperone with a wide array of client proteins, including the tumor suppressor p53. Now the structure and interaction of p53 DNA-binding domain with full-length Hsp90 or Hsp90 fragments have been studied by NMR and other biophysical methods. The results indicate that p53 interacts with multiple domains of Hsp90 and adopts a native-like state.
- Franz Hagn
- Stephan Lagleder
- Horst Kessler
