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The eukaryotic large ribosomal subunit (60S) is an essential component of the cytosolic 80S ribosome in eukaryotes. It consists of three rRNA molecules—28S, 5.8S, and 5S rRNAs—and approximately 47–49 proteins. The primary function of the 60S subunit is to catalyze peptide bond formation during protein synthesis via its peptidyl transferase center—a reaction fundamental for translating mRNA into polypeptides. The structure also contains sites for tRNA binding and forms part of the exit tunnel through which nascent polypeptides emerge. Drugs such as cycloheximide inhibit its activity by blocking elongation during translation. While it shares functional similarities with the prokaryotic large (50S) subunit, it is larger and more complex due to additional RNA expansion segments and unique proteins found only in eukaryotes. Disruption or dysregulation can contribute to diseases such as cancer or rare inherited disorders known as ribosomopathies. Because global inhibition leads to cell death across tissues, direct pharmacological targeting carries significant safety concerns except under controlled experimental conditions.
Inhibition of peptide bond formation by binding to the peptidyl transferase center
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