The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopy.

@article{Sreeramulu2009TheHC,
  title={The human Cdc37.Hsp90 complex studied by heteronuclear NMR spectroscopy.},
  author={Sridhar Sreeramulu and Hendrik R. A. Jonker and Thomas Langer and Christian Richter and C. Roy D. Lancaster and Harald Schwalbe},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 6},
  pages={3885-96}
}
The cell division cycle protein 37 (Cdc37) and the 90-kDa heat shock protein (Hsp90) are molecular chaperones, which are crucial elements in the protein signaling pathway. The largest class of client proteins for Cdc37 and Hsp90 are protein kinases. The catalytic domains of these kinases are stabilized by Cdc37, and their proper folding and functioning is dependent on Hsp90. Here, we present the x-ray crystal structure of the 16-kDa middle domain of human Cdc37 at 1.88 angstroms resolution and… CONTINUE READING

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