Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange

@article{Brehmer2001TuningOC,
  title={Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange},
  author={Dirk Brehmer and Stefan R{\"u}diger and Claudia S. G{\"a}ssler and Dagmar Klostermeier and Lars Packschies and Jochen Reinstein and Matthias P. Mayer and Bernd Bukau},
  journal={Nature Structural Biology},
  year={2001},
  volume={8},
  pages={427-432}
}
The Hsp70 chaperone activity in protein folding is regulated by ATP-controlled cycles of substrate binding and release. Nucleotide exchange plays a key role in these cycles by triggering substrate release. Structural searches of Hsp70 homologs revealed three structural elements within the ATPase domain: two salt bridges and an exposed loop. Mutational analysis showed that these elements control the dissociation of nucleotides, the interaction with exchange factors and chaperone activity… CONTINUE READING
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The Hsp70 chaperone activity in protein folding is regulated by ATP - controlled cycles of substrate binding and release .
The Hsp70 chaperone activity in protein folding is regulated by ATP - controlled cycles of substrate binding and release .
The Hsp70 chaperone activity in protein folding is regulated by ATP - controlled cycles of substrate binding and release .
Molecular ChaperonesGene product plays role in biological processprotein folding
The Hsp70 chaperone activity in protein folding is regulated by ATP - controlled cycles of substrate binding and release .
The Hsp70 chaperone activity in protein folding is regulated by ATP - controlled cycles of substrate binding and release .
The Hsp70 chaperone activity in protein folding is regulated by ATP - controlled cycles of substrate binding and release .
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