Post-translational modification of heat-shock protein 90: impact on chaperone function.

@article{Scroggins2007PosttranslationalMO,
  title={Post-translational modification of heat-shock protein 90: impact on chaperone function.},
  author={Bradley T. Scroggins and Leonard M. Neckers},
  journal={Expert opinion on drug discovery},
  year={2007},
  volume={2 10},
  pages={1403-14}
}
Heat-shock protein 90 (Hsp90) is a molecular chaperone required for the stability and function of many signaling proteins that are often activated, mutated or overexpressed in cancer cells and that underly cancer cell proliferation and survival. Hsp90 is a conformationally flexible protein that associates with a distinct set of cochaperones depending on ATP or ADP occupancy of an N-terminal binding pocket. Nucleotide exchange and ATP hydrolysis by Hsp90 itself, with the assistance of… CONTINUE READING
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