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Ribosomal protein lateral stalk subunit P2 (RPLP2) is an acidic phosphoprotein component of the eukaryotic large (60S) ribosomal subunit, integral to the ribosomal stalk structure. It interacts with P0 and P1 proteins to form a pentameric complex facilitating the recruitment and positioning of translation factors at the ribosome’s GTPase center, which is essential for the elongation phase of protein synthesis. RPLP2 is structurally a functional equivalent to the E. coli L7/L12 protein and belongs to the L12P family. It is implicated in modulation of translational activity and cell proliferation rates. While not typically a direct drug target, the protein’s conserved C-terminal region mediates interactions with ribosome-inactivating proteins such as ricin and trichosanthin, which exploit this interaction to inhibit protein synthesis. RPLP2 is also recognized as an antigen in renal carcinoma, though its broader role in human disease is primarily linked to its function in the ribosome
Not directly targeted by drugs; mechanism for toxins/RIPs involves binding to the conserved C-terminal domain and inactivating the ribosome by preventing elongation factor binding
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