Final answer:
Preventing Hsp-90 from binding substrates could destabilize various proteins, including hormone receptors and signaling molecules, potentially disrupting cell signaling and other cellular functions. This action is being explored in cancer therapy to target proteins essential for cancer cell growth.
Step-by-step explanation:
The result of a drug which prevents Hsp-90 from binding substrates would likely lead to a disruption in the protein stabilization and maturation processes that Hsp-90 is involved in. Hsp-90 acts as a molecular chaperone, ensuring proper protein folding and preventing protein aggregation, particularly under stress conditions such as increased temperatures. If Hsp-90 is inhibited, its substrates, which include various protein clients such as hormone receptors and signaling proteins, may become unstable and dysfunctional. This could, in turn, lead to a range of cellular dysfunctions, as proteins play critical roles in almost all cellular processes. For example, if Hsp-90 cannot bind to hormone receptors, these receptors may not be able to properly respond to hormonal signals, potentially disrupting cell signaling pathways. Similarly, if signaling proteins cannot be properly stabilized by Hsp-90, they may not function correctly, which could impact cell growth, division, and survival processes. In the context of cancer therapy, Hsp-90 inhibitors are currently being explored as a way to target and destabilize proteins that are crucial for cancer cell growth and survival.