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Structures and Ribosomal Interaction of Ribosome-Inactivating Proteins

Centre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China
Author to whom correspondence should be addressed.
Academic Editor: Els Van Damme
Molecules 2016, 21(11), 1588;
Received: 10 October 2016 / Revised: 9 November 2016 / Accepted: 15 November 2016 / Published: 21 November 2016
PDF [3993 KB, uploaded 22 November 2016]


Ribosome-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
Keywords: ribosome-inactivating proteins; RNA N-glycosidases; ribosome; P proteins; ribosomal interaction ribosome-inactivating proteins; RNA N-glycosidases; ribosome; P proteins; ribosomal interaction

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Shi, W.-W.; Mak, A.N.; Wong, K.-B.; Shaw, P.-C. Structures and Ribosomal Interaction of Ribosome-Inactivating Proteins. Molecules 2016, 21, 1588.

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