Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70.

@article{Carrello2004InteractionOT,
  title={Interaction of the Hsp90 cochaperone cyclophilin 40 with Hsc70.},
  author={Amerigo Carrello and Rudi Kenneth Allan and Sarah L. Morgan and Barbara A. L. Owen and Danny Mok and Bryan K Ward and Rodney F. Minchin and David O. Toft and Thomas Ratajczak},
  journal={Cell stress & chaperones},
  year={2004},
  volume={9 2},
  pages={167-81}
}
The high-affinity ligand-binding form of unactivated steroid receptors exists as a multicomponent complex that includes heat shock protein (Hsp)90; one of the immunophilins cyclophilin 40 (CyP40), FKBP51, or FKBP52; and an additional p23 protein component. Assembly of this heterocomplex is mediated by Hsp70 in association with accessory chaperones Hsp40, Hip, and Hop. A conserved structural element incorporating a tetratricopeptide repeat (TPR) domain mediates the interaction of the… CONTINUE READING

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