Heat shock protein 60kDa (Hsp60) is a chaperone classically believed to be involved in assisting the correct folding of other
mitochondrial proteins. Hsp60 also plays a role in cytoprotection against cell stressors, displaying for example, antiapoptotic potential.
Despite the plethora of studies devoted to the mechanism of Hsp60’s function, especially in prokaryotes, fundamental issues still remain
unexplored, including the definition of its role in cancer. Key questions still unanswered pertain to the differences in structure-function
features that might exist between the well-studied prokaryotic GroEL and the largely unexplored eukaryotic Hsp60 proteins. In this article
we discuss these differences in sequence, structure, and roles of Hsp60, focusing on the human ortholog with the view of devising
compounds to block its ability to favour tumor-cell growth and survival. Compounds currently known to directly or indirectly affect
Hsp60 functions, such as protein folding, HIF-1α accumulation, or Hsp60-induced cell proliferation, are discussed along with strategies
that might prove effective for developing Hsp60-targeting drugs for anticancer therapy.
Keywords: Hsp60, chaperonin, functional domains, binding pocket, compound docking, epolactaene, drug design, cancer treatment
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