HSP90AA1 and cancer: Therefore, the following can be hypothesized: HSP90 has low-affinity interactions with client proteins, which are regulated by low-affinity binding and the release of ATP and ADP, but upon mutation or deregulation, which is present in the cancer phenotype, many of these client proteins may display atypically stable interactions with HSP90, representing the active state that has a higher affinity for inhibitor drugs [13].