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Eukaryotic ribosomal 60S subunit (60S ribosomal subunit)

Target
60S ribosomal subunit
Molecular classification
Ribosomal subunit, Ribonucleoprotein complex, Macromolecular machine, Ribosome component
01

Overview

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].

Other names
60S large subunitlarge ribosomal subunit (60S)eukaryotic 60S subunitribosomal large subunit (eukaryotic)60S subunit
02

Mechanism of action

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

03

Biological functions

Protein synthesis (translation)Peptide bond formationmRNA translationPolypeptide chain elongation
04

Disease associations

CancerRibosomopathies (congenital disorders of ribosome biogenesis/function)Infection (antibiotic targeting)Other (disorders of protein synthesis)
05

Safety considerations

Inhibition leads to global suppression of protein synthesis, causing cytotoxicity in both normal and cancer cellsOff-target toxicity due to lack of selectivity (inhibitors can affect all dividing/active cells)Potential immunogenic responses to ribosomal protein alterationsBroad essentiality limits therapeutic window
06

Interacting drugs

Cycloheximide

3 more in the full profile.

07

Biomarkers

Mutations or deletions in rRNA or ribosomal proteins (e.g., diagnostic in Diamond-Blackfan anemia)Ribosomal protein overexpression as a cancer biomarkerrRNA modification profiles

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