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The **eukaryotic large ribosomal subunit 60S** is one of the two subunits that together form the eukaryotic 80S ribosome, the principal cellular machine for translating messenger RNA (mRNA) into protein. The 60S subunit is a large ribonucleoprotein complex, composed of 47 proteins and three ribosomal RNAs (28S, 5.8S, and 5S rRNA in humans), assembled into a highly intricate three-dimensional structure. It houses the **peptidyl transferase center**, which catalyzes peptide bond formation—making it the primary engine of protein synthesis in the cell. The subunit also contains sites for tRNA accommodation and the peptide exit tunnel, as well as binding domains for translation factors and quality control machinery. Its function and composition are highly conserved but elaborated in eukaryotes, with additional protein and RNA expansion segments distinguishing it from prokaryotic counterparts. The 60S subunit is a **critical therapeutic target** for certain antibiotics that exploit the differences between eukaryotic and prokaryotic ribosomes for selective inhibition, although inhibition in higher eukaryotes (such as humans) leads to potent cytotoxic effects due to the essential nature of protein synthesis. Dysfunction or mutations in the 60S subunit underlie several diseases known as ribosomopathies, and aberrant biogenesis or activity is linked to cancer and other pathologies.
Inhibition of protein synthesis via blockade of the peptidyl transferase activity or movement of tRNA on the ribosome Interference with nascent peptide translocation or GTPase-associated factor binding
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