The molecular chaperone protein Hsp70 is centrally involved in cellular homeostasis by assisting in the folding and degradation of protein substrates. Hsp70 is joined by co-chaperones, such as Hsp110, which contribute to specialized tasks of the Hsp70 complex. Imbalances of this heat shock protein system are believed to be involved with the deregulation of cancer pathways and other human diseases. Better understanding of how these heat shock proteins work at the molecular level, which has been investigated using molecular docking tools, will give more clues about biological function. Simulating the formation and function of Hsp70 based chaperone complexes could provide new information about the control and regulation of these processes and well as new areas of exploration for drug discovery.
Stetz, Gabrielle and Verkhivker, Gennady M., "Dancing Through Life: Allosteric Transitions and Structural Analysis of Hsp70 and Hsp110 Chaperone Proteins" (2014). Student Research Day Abstracts and Posters. 57.