Crystal structures of the 70-kDa heat shock proteins in domain disjoining conformation.

@article{Chang2008CrystalSO,
  title={Crystal structures of the 70-kDa heat shock proteins in domain disjoining conformation.},
  author={Y Chang and Yuh-Ju Sun and Chung Wang and C. Hsiao},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 22},
  pages={15502-11}
}
The 70-kDa heat shock proteins (Hsp70s) are highly conserved ATP-dependent molecular chaperones composed of an N-terminal nucleotide binding domain (NBD) and a C-terminal protein substrate binding domain (SBD) in a bilobate structure. Interdomain communication and nucleotide-dependent structural motions are critical for Hsp70 chaperone functions. Our understanding of these functions remains elusive due to insufficient structural information on intact Hsp70s that represent the different states… CONTINUE READING
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