20S Proteasome Core + 'Compound 1' Inhibitor

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The cellular proteasome complex plays a vital role in protein degradation, with multiple sites within its core particle driving various reactions (Coux et al. 1996). These include the chymotrypsin-like site β5, which cleaves large hydrophobic residues and has been linked to cancer cell proliferation (Groll et al. 1996), as well as a potential target for inhibition (Blackburn et al. 2010). Bortezomib limits proteasome activity by binding reversibly to the enzyme active site, but recent discoveries suggest that 'compound 1' may act as a rapid-equilibrium inhibitor with more selective and controlled binding (Blackburn et al. 2010). Although the interaction between β5 and 'compound 1' is not fully understood, its reversible mechanism can be likened to Bortezomib's, paving the way for further study of the compound's potential in cancer treatment development (Blackburn et al. 2010).