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Toxins 2018, 10(8), 335; https://doi.org/10.3390/toxins10080335

Structural and Functional Investigation and Pharmacological Mechanism of Trichosanthin, a Type 1 Ribosome-Inactivating Protein

Centre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Sha Tin New Town, Hong Kong, China
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Received: 25 July 2018 / Revised: 16 August 2018 / Accepted: 17 August 2018 / Published: 20 August 2018
(This article belongs to the Special Issue Toxicity of Plant Toxins in Medical Herbs)
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Abstract

Trichosanthin (TCS) is an RNA N-glycosidase that depurinates adenine-4324 in the conserved α-sarcin/ricin loop (α-SRL) of rat 28 S ribosomal RNA (rRNA). TCS has only one chain, and is classified as type 1 ribosome-inactivating protein (RIP). Our structural studies revealed that TCS consists of two domains, with five conserved catalytic residues Tyr70, Tyr111, Glu160, Arg163 and Phe192 at the active cleft formed between them. We also found that the structural requirements of TCS to interact with the ribosomal stalk protein P2 C-terminal tail. The structural analyses suggest TCS attacks ribosomes by first binding to the C-terminal domain of ribosomal P protein. TCS exhibits a broad spectrum of biological and pharmacological activities including anti-tumor, anti-virus, and immune regulatory activities. This review summarizes an updated knowledge in the structural and functional studies and the mechanism of its multiple pharmacological effects. View Full-Text
Keywords: TCS; ribosome-inactivating protein; ribosomal stalk P protein; multiple pharmacological activities; mechanism TCS; ribosome-inactivating protein; ribosomal stalk P protein; multiple pharmacological activities; mechanism
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Shi, W.-W.; Wong, K.-B.; Shaw, P.-C. Structural and Functional Investigation and Pharmacological Mechanism of Trichosanthin, a Type 1 Ribosome-Inactivating Protein. Toxins 2018, 10, 335.

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