Characterization of D10S and K71E mutants of human cytosolic hsp70.

@article{Rajapandi1998CharacterizationOD,
  title={Characterization of D10S and K71E mutants of human cytosolic hsp70.},
  author={T Rajapandi and Chenglin Wu and Evan Eisenberg and Lois E. Greene},
  journal={Biochemistry},
  year={1998},
  volume={37 20},
  pages={
          7244-50
        }
}
To determine the effect of mutations at the nucleotide-binding site of recombinant Hsp70 on its interaction with protein and peptide substrates, point mutations were made at D10 and K71, two residues at the active site. The D10S mutation weakened both ATP and ADP binding, while the K71E mutation weakened only ATP binding. In binding experiments using Hsp70 with no bound nucleotide, the mutated Hsp70s interacted with clathrin and peptide just like the wild-type Hsp70. However, the D10 mutation… CONTINUE READING

Citations

Publications citing this paper.
SHOWING 1-10 OF 14 CITATIONS

Hsp72 chaperone function is dispensable for protection against stress-induced apoptosis

  • Cell Stress and Chaperones
  • 2008
VIEW 8 EXCERPTS
CITES BACKGROUND & METHODS
HIGHLY INFLUENCED

Centrosome-intrinsic mechanisms modulate centrosome integrity during fever

VIEW 3 EXCERPTS
CITES METHODS & BACKGROUND
HIGHLY INFLUENCED

Hsp70 dynamics in vivo: effect of heat shock and protein aggregation.

  • Journal of cell science
  • 2004
VIEW 4 EXCERPTS
CITES BACKGROUND & METHODS

A protective Hsp70-TLR4 pathway in lethal oxidant lung injury.

  • Journal of immunology
  • 2013
VIEW 1 EXCERPT
CITES BACKGROUND