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Molecules 2016, 21(11), 1588; doi:10.3390/molecules21111588

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
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Academic Editor: Els Van Damme
Received: 10 October 2016 / Revised: 9 November 2016 / Accepted: 15 November 2016 / Published: 21 November 2016
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Abstract

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.-S.; Wong, K.-B.; Shaw, P.-C. Structures and Ribosomal Interaction of Ribosome-Inactivating Proteins. Molecules 2016, 21, 1588.

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