Heterogeneous binding of the SH3 client protein to the DnaK molecular chaperone.

@article{Lee2015HeterogeneousBO,
  title={Heterogeneous binding of the SH3 client protein to the DnaK molecular chaperone.},
  author={Jung Ho Lee and Dongyu Zhang and Christopher Hughes and Yusuke Okuno and Ashok Sekhar and Silvia Cavagnero},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2015},
  volume={112 31},
  pages={E4206-15}
}
The molecular chaperone heat shock protein 70 (Hsp70) plays a vital role in cellular processes, including protein folding and assembly, and helps prevent aggregation under physiological and stress-related conditions. Although the structural changes undergone by full-length client proteins upon interaction with DnaK (i.e., Escherichia coli Hsp70) are… CONTINUE READING