A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells.

@article{Chiosis2001ASM,
  title={A small molecule designed to bind to the adenine nucleotide pocket of Hsp90 causes Her2 degradation and the growth arrest and differentiation of breast cancer cells.},
  author={Gabriela Chiosis and M N Timaul and Brian Lucas and Pamela N. Munster and Fuzhong F. Zheng and Laura Sepp-Lorenzino and Neal Rosen},
  journal={Chemistry & biology},
  year={2001},
  volume={8 3},
  pages={289-99}
}
BACKGROUND The Hsp90s contain a conserved pocket that binds ATP/ADP and plays an important role in the regulation of chaperone function. Occupancy of this pocket by several natural products (geldanamycin (GM) and radicicol) alters Hsp90 function and results in the degradation of a subset of proteins (i.e. steroid receptors, Her2, Raf). We have used the structural features of this pocket to design a small molecule inhibitor of Hsp90. RESULTS The designed small molecule PU3 competes with GM for… CONTINUE READING
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