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• W2530254443 endingPage "296" @default.
• W2530254443 startingPage "296" @default.
• W2530254443 abstract "Ricin is a type 2 ribosome-inactivating protein (RIP), containing a catalytic A chain and a lectin-like B chain. It inhibits protein synthesis by depurinating the N-glycosidic bond at α-sarcin/ricin loop (SRL) of the 28S rRNA, which thereby prevents the binding of elongation factors to the GTPase activation center of the ribosome. Here, we present the 1.6 Å crystal structure of Ricin A chain (RTA) complexed to the C-terminal peptide of the ribosomal stalk protein P2, which plays a crucial role in specific recognition of elongation factors and recruitment of eukaryote-specific RIPs to the ribosomes. Our structure reveals that the C-terminal GFGLFD motif of P2 peptide is inserted into a hydrophobic pocket of RTA, while the interaction assays demonstrate the structurally untraced SDDDM motif of P2 peptide contributes to the interaction with RTA. This interaction mode of RTA and P protein is in contrast to that with trichosanthin (TCS), Shiga-toxin (Stx) and the active form of maize RIP (MOD), implying the flexibility of the P2 peptide-RIP interaction, for the latter to gain access to ribosome." @default.
• W2530254443 created "2016-10-21" @default.
• W2530254443 creator A5031994389 @default.
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• W2530254443 date "2016-10-13" @default.
• W2530254443 modified "2023-09-28" @default.
• W2530254443 title "Crystal Structure of Ribosome-Inactivating Protein Ricin A Chain in Complex with the C-Terminal Peptide of the Ribosomal Stalk Protein P2" @default.
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• W2530254443 doi "https://doi.org/10.3390/toxins8100296" @default.
• W2530254443 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5086656" @default.
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