Structure elucidation of the Hsp90-Cdc37 complex

The “cell division cycle” protein 37 (Cdc37) and the 90 kDa heat shock protein (Hsp90) are molecular chaperones, which play important roles in the protein signal transduction. Cdc37 and Hsp90 are chaperones for proteinkinase. We determined the crystal structure of the middle domain of Cdc37 with a resolution of 1.88 Å and the NMR structure of its complex with the 23 kDa N-terminal domain of human Hsp90.

  • Sreeramulu, S., Jonker, H. R. A., Langer, T., Richter, C., Lancaster, C. R. D. & Schwalbe, H. The human Cdc37 center dot Hsp90 complex studied by heteronuclear NMR spectroscopy. J. Biol. Chem. 284, 3885-3896 (2009)
  • Molecular mechanism of inhibition of the human protein complex Cdc37-Hsp90, a kinome chaperone-cochaperone, by triterpene celastrol. Angew. Chem. 48, 5853-5855 (2009)