Eukaryotic 60S ribosomal subunit (60S ribosomal subunit)

The Eukaryotic 60S ribosomal subunit is the large component of the eukaryotic 80S ribosome, a macromolecular complex responsible for protein synthesis in cells[1][2][3][4][6][7]. It consists of three ribosomal RNA molecules (28S, 5.8S, and 5S rRNAs) and approximately 46 ribosomal proteins in humans[3][6]. The 60S subunit catalyzes peptide bond formation at its peptidyl transferase center and provides the polypeptide exit tunnel through which new proteins emerge. It also contains functional sites for tRNA binding (A, P, and E sites) and interacts with translation factors and GTPases necessary for translation[1][4][10]. The biogenesis of the 60S subunit is a complex, highly regulated process involving many assembly factors and occurs co-transcriptionally in the nucleolus[3][4]. Inhibitors that target the 60S subunit block protein synthesis and display antiproliferative, cytotoxic, or antimicrobial activity, making the 60S ribosomal subunit a therapeutic target in oncology and infectious diseases, but with significant toxicity due to its critical role in all proliferating cells[7]. Alterations in ribosome composition or function (e.g., mutated ribosomal proteins, rRNA modifications) are implicated in cancers and ribosomopathies[2][6]. The structure of the human 60S subunit has been characterized at near atomic resolution, revealing numerous RNA/protein modifications and complex architecture that distinguishes it from prokaryotic counterparts[2]. Note: The 60S ribosomal subunit is a macromolecular complex, not a single protein or classical receptor/enzyme, but it is a validated molecular target for several drugs and investigational therapeutics.

Other names

Large ribosomal subunit (60S)Ribosomal large subunit (60S)60S large subunit

Inhibition of peptide bond formation (by binding peptidyl transferase center); Inhibition of translocation or elongation during translation