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The **eukaryotic ribosomal 60S subunit** is the large component of the eukaryotic cytosolic ribosome, a fundamental ribonucleoprotein complex responsible for cytoplasmic protein synthesis. It is composed of three ribosomal RNAs (28S, 5.8S, and 5S rRNAs) and approximately 47-49 proteins, forming a structure essential for catalyzing peptide bond formation through the peptidyl transferase center[2][3][7][8]. The 60S subunit also features important functional regions such as the polypeptide exit tunnel, the A-, P-, and E-sites for tRNA binding, and the GTPase-associated center for interaction with key translation factors[2][5]. It joins the 40S small subunit to assemble the functional 80S ribosome and participates in translation elongation and termination[2][7]. Being indispensable for protein biosynthesis, it is a critical therapeutic target for a range of antibiotics and toxins that halt its function, and its dysfunction is implicated in various cancers, inherited ribosomopathies, and cellular responses to infection[2][3][5][8].
Inhibition of peptide bond formation (e.g., cycloheximide blocks the translocation step in translation on the 60S) Inhibition of ribosomal function by rRNA depurination (e.g., ricin modifies a single adenine in the 28S rRNA, disabling the peptidyl transferase center) Disruption of ribosome assembly or function
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