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Ribosome-inactivating protein

A ribosome-inactivating protein (RIP) is a protein synthesis inhibitor that acts at the eukaryotic ribosome. This protein family describes a large family of such proteins that work by acting as rRNA N-glycosylase. They inactivate 60S ribosomal subunits by an N-glycosidic cleavage, which releases a specific adenine base from the sugar-phosphate backbone of 28S rRNA. RIPs exist in bacteria and plants.

Classification
Ribosome-inactivating proteins (RIPs) are separated into the following types based on protein domain composition: • Type III: RIPs-III are separated into two subgroups. • Shiga toxin belongs to its own group, as the carbohydrate-binding ability (B5 domain) evolved separately and the catalytic domain is closer to type I (A) RIPs than to type II (AB). == Examples ==
Examples
Examples include: • Type A: Plant antiviral proteins (Beetin, Saporin, Pokeweed antiviral protein (Phytolacca americana), Trichosanthin), a Spiroplasma toxin • Type AB: Abrin, Ricin, Viscumin (European mistletoe) • Type AC: • Type AD: • Shiga toxin == References ==
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