Visualization and functional analysis of the oligomeric states of Escherichia coli heat shock protein 70 (Hsp70/DnaK)

@article{Thompson2011VisualizationAF,
  title={Visualization and functional analysis of the oligomeric states of Escherichia coli heat shock protein 70 (Hsp70/DnaK)},
  author={Andrea D. Thompson and Steffen M. Bernard and Georgios Skiniotis and Jason E. Gestwicki},
  journal={Cell Stress and Chaperones},
  year={2011},
  volume={17},
  pages={313-327}
}
The molecular chaperone DnaK binds to exposed hydrophobic segments in proteins, protecting them from aggregation. DnaK interacts with protein substrates via its substrate-binding domain, and the affinity of this interaction is allosterically regulated by its nucleotide-binding domain. In addition to regulating interdomain allostery, the nucleotide state has been found to influence homo-oligomerization of DnaK. However, the architecture of oligomeric DnaK and its potential functional relevance… CONTINUE READING
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