ribosome-inactivating protein

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ribosome-inactivating protein (RIP)

one of a variety of enzymes that cleave the N-glycosidic bond of adenine in a specific ribosomal RNA sequence. Type 1 RIPs are single-chain proteins. Some type 2 RIPs, such as ricin, possess a galactose-specific lectin domain that binds to cell surfaces, making them potent toxins.
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Four major lectin families, namely, the legume lectins, the chitin-binding lectins composed of hevein domains, the type2 ribosome-inactivating proteins and the monocot mannose-binding lectins comprise the majority of all currently known plant lectins (Van Damme et al.
A variety of proteins like ubiquitin-like proteases, proteoglycans, ribosome-inactivating proteins, antifungal proteins and lectins with immunomodulatory, antitumor, antifungal and hypotensive activities have been isolated from mushrooms (Wang et al.
Recently, structure biology studies and X-ray crystallography of the various isoforms of mistletoe lectins, which belong to the type II ribosome-inactivating proteins (RIPII), have led to new insights into substrate preferences and substrate binding.