The 70 kilodalton heat shock proteins (Hsp70s) are a family of conserved ubiquitously expressedheat shock proteins. Proteins with similar structure exist in virtually all living organisms. The Hsp70s are an important part of the cell's machinery for protein folding, and help to protect cells from stress. When not interacting with a substrate peptide, Hsp70 is usually in an ATP bound state. Hsp70 by itself is characterized by a very weak ATPase activity, such that spontaneous hydrolysis will not occur for many minutes. As newly synthesized proteins emerge from the ribosomes, the substrate binding domain of Hsp70 recognizes sequences of hydrophobic amino acid residues, and interacts with them. This spontaneous interaction is reversible, and in the ATP bound state Hsp70 may relatively freely bind and release peptides. However, the presence of a peptide in the binding domain stimulates the ATPase activity of Hsp70, increasing its normally slow rate of ATP hydrolysis.

1. "The disordered amino-terminus of SIMPL interacts with members of the 70-kDa heat-shock protein family." Haag Breese E., Uversky V.N., Georgiadis M.M., Harrington M.A.DNA Cell Biol. 25:704-714(2006)
2. "Hsp70 interacts with the retroviral restriction factor TRIM5alpha and assists the folding of TRIM5alpha." Hwang C.Y., Holl J., Rajan D., Lee Y., Kim S., Um M., Kwon K.S., Song B. J. Biol. Chem. 285:7827-7837(2010)