Heat shock 70 kDa protein 1A (HSPA1A)

Molecular chaperone implicated in a wide array of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality management system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation.

The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a parasite while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state.