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60S ribosomal protein L7 (RPL7) is a conserved structural protein of the large (60S) ribosomal subunit in eukaryotic cells, encoded by the RPL7 gene[1][3][5]. It binds RNA—including G-rich regions of 28S rRNA and various mRNAs—and contains an N-terminal basic region-leucine zipper (BZIP)-like domain enabling homodimerization, stable DNA and RNA binding, and potential regulatory functions in translation[1][4][5]. RPL7 also supports ribosome association with the endoplasmic reticulum, and evidence suggests it mediates cellular co-factor activity during HIV-1 viral assembly via direct interaction with the Gag protein[3]. As an autoantigen, RPL7 is implicated in systemic autoimmune diseases, including systemic lupus erythematosus[1][5]. Disruption of RPL7 function may contribute to oncogenic processes, but this remains under investigation[3]. There are no approved drugs targeting RPL7, and its essential role in protein synthesis means it is not considered a classical therapeutic target[1][5].
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