Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interactions.

@article{Yun2004NovobiocinIA,
  title={Novobiocin induces a distinct conformation of Hsp90 and alters Hsp90-cochaperone-client interactions.},
  author={Bo-Geon Yun and Wenjun Huang and Natalie R Leach and Steven D. Hartson and Robert L. Matts},
  journal={Biochemistry},
  year={2004},
  volume={43 25},
  pages={
          8217-29
        }
}
Hsp90 functions to facilitate the folding of newly synthesized and denatured proteins. Hsp90 function is modulated through its interactions with cochaperones and the binding and hydrolysis of ATP. Recently, novobiocin has been shown to bind to a second nucleotide binding site located within the C-terminal domain of Hsp90. In this report, we have examined the effect of novobiocin on Hsp90 function in reticulocyte lysate. Novobiocin specifically inhibited the maturation of the heme-regulated… CONTINUE READING
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