Structures and Ribosomal Interaction of Ribosome-Inactivating Proteins
AbstractRibosome-inactivating proteins (RIPs) including ricin, Shiga toxin, and trichosanthin, are RNA N-glycosidases that depurinate a specific adenine residue (A-4324 in rat 28S ribosomal RNA, rRNA) in the conserved α-sarcin/ricin loop (α-SRL) of rRNA. RIPs are grouped into three types according to the number of subunits and the organization of the precursor sequences. RIPs are two-domain proteins, with the active site located in the cleft between the N- and C-terminal domains. It has been found that the basic surface residues of the RIPs promote rapid and specific targeting to the ribosome and a number of RIPs have been shown to interact with the C-terminal regions of the P proteins of the ribosome. At present, the structural basis for the interaction of trichosanthin and ricin-A chain toward P2 peptide is known. This review surveys the structural features of the representative RIPs and discusses how they approach and interact with the ribosome. View Full-Text
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Shi, W.-W.; Mak, A.N.-S.; Wong, K.-B.; Shaw, P.-C. Structures and Ribosomal Interaction of Ribosome-Inactivating Proteins. Molecules 2016, 21, 1588.
Shi W-W, Mak AN-S, Wong K-B, Shaw P-C. Structures and Ribosomal Interaction of Ribosome-Inactivating Proteins. Molecules. 2016; 21(11):1588.Chicago/Turabian Style
Shi, Wei-Wei; Mak, Amanda N.-S.; Wong, Kam-Bo; Shaw, Pang-Chui. 2016. "Structures and Ribosomal Interaction of Ribosome-Inactivating Proteins." Molecules 21, no. 11: 1588.
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