structures and ribosomal interaction of ribosome-inactivating proteins

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ID: 209995
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.
Reference Key
shi2016moleculesstructures Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Wei-Wei Shi;Amanda Nga-Sze Mak;Kam-Bo Wong;Pang-Chui Shaw
Journal Journal of ethnopharmacology
Year 2016
DOI
10.3390/molecules21111588
URL
http://www.mdpi.com/1420-3049/21/11/1588
Keywords
ribosome-inactivating proteins

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