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Ribonuclease T2 is a highly conserved endoribonuclease enzyme that cleaves single-stranded RNA, producing nucleotides via a 2’,3’-cyclic phosphate intermediate. Human RNase T2 is localized primarily in lysosomes and is involved in the degradation of endogenous and exogenous RNAs, immune modulation, and tumor suppression. The enzyme shows a typical α+β fold and contains two conserved catalytic motifs vital for activity; active sites depend on several key histidine residues. RNase T2 plays a role in immune defense, tissue remodeling, and apoptosis, and its reduced expression or mutation has been linked to cancer progression, autoimmune diseases, and inherited neurological diseases such as leukoencephalopathy. No approved drugs specifically target RNase T2, but its modulation could have therapeutic potential in cancer, inflammation, and infection.
Inhibition of enzymatic RNA cleavage (e.g., by zinc or mutation of active site); potential immunomodulatory or anti-inflammatory activity if therapeutically exploited.
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