Molecular Characterization of the Recombinant A-chain of a Type Ⅱ Ribosome-Inactivating Protein (RIP) from Viscum album coloratum and Structural Basis on its Ribosome-Inactivating Activity and the Sugar-binding Properties of the B-chain
Mistletoe (Viscum album) lectins, which are classified as a type Ⅱ ribosome-inactivating protein (RIP) due to their unique biological function and the potential medical and therapeutic application in cancer cells, receive a rising attention. The heterodimeric glycoproteins contain the A-chain with c...
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Published in | BMB reports Vol. 39; no. 5; pp. 560 - 570 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Korea (South)
30.09.2006
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Subjects | |
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Abstract | Mistletoe (Viscum album) lectins, which are classified as a type Ⅱ ribosome-inactivating protein (RIP) due to their unique biological function and the potential medical and therapeutic application in cancer cells, receive a rising attention. The heterodimeric glycoproteins contain the A-chain with catalytic activity and the B-chain with sugar binding properties. In recent years, studies involving the lectins from the white berry European mistletoe (Viscum album) and the yellow berry Korean mistletoe (Viscum album coloratum) have been described. |
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AbstractList | Mistletoe (Viscum album) lectins, which are classified as a type II ribosome-inactivating protein (RIP) due to their unique biological function and the potential medical and therapeutic application in cancer cells, receive a rising attention. The heterodimeric glycoproteins contain the Achain with catalytic activity and the B-chain with sugar binding properties. In recent years, studies involving the lectins from the white berry European mistletoe (Viscum album) and the yellow berry Korean mistletoe (Viscum album coloratum) have been described. However, the detailed mechanism in exerting unique cytotoxic effect on cancer cells still remains unclear. Here, we aim to understand and define the molecular basis and biological effects of the type II RIPs, through the studies of the recombinant Korean mistletoe lectin. To this end, we expressed, purified the recombinant Korean mistletoe lectin (rKML), and investigated its molecular characteristics in vitro, its cytotoxicity and ability to induce apoptotic cell death in cancer cells. To gain structural basis for its catalytic activity and sugar binding properties, we performed homology modeling studies based on the high degree of sequence identity and conserved secondary structure prediction between Korean and European, Himalayan mistletoe lectins, and Ricin. Mistletoe (Viscum album) lectins, which are classified as a type Ⅱ ribosome-inactivating protein (RIP) due to their unique biological function and the potential medical and therapeutic application in cancer cells, receive a rising attention. The heterodimeric glycoproteins contain the A-chain with catalytic activity and the B-chain with sugar binding properties. In recent years, studies involving the lectins from the white berry European mistletoe (Viscum album) and the yellow berry Korean mistletoe (Viscum album coloratum) have been described. |
Author | Yoon, H.S. (Nanyang Technological University, Singapore), E-mail: hsyoon@ntu.edu.sg Nanga, Ravi Prakash Reddy (Nanyang Technological University, Singapore) Song, S.K. (Handong University, Pohang, Republic of Korea) Song, J.H. (Handong University, Pohang, Republic of Korea) Ye, Wenhui (Nanyang Technological University, Singapore) Kang, C.B. (Nanyang Technological University, Singapore) |
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Snippet | Mistletoe (Viscum album) lectins, which are classified as a type Ⅱ ribosome-inactivating protein (RIP) due to their unique biological function and the... Mistletoe (Viscum album) lectins, which are classified as a type II ribosome-inactivating protein (RIP) due to their unique biological function and the... |
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SubjectTerms | Amino Acid Sequence Apoptosis Carbohydrates - chemistry Catalytic Domain Cell Line, Tumor Cell Survival - drug effects Circular Dichroism Glycosylation Humans Inhibitory Concentration 50 LECTINAS LECTINE LECTINS Magnetic Resonance Spectroscopy Models, Molecular Molecular Sequence Data N-Glycosyl Hydrolases - metabolism Plant Preparations - chemistry Plant Preparations - metabolism Plant Preparations - pharmacology Plant Proteins - chemistry Plant Proteins - genetics Plant Proteins - metabolism Plant Proteins - pharmacology Protein Folding Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Recombinant Proteins - pharmacology Ribosome Inactivating Proteins Ribosome Inactivating Proteins, Type 2 Ribosome-inactivating protein Ricin - chemistry Ricin - genetics Structural Homology, Protein Sugar binding Toxins, Biological - chemistry Toxins, Biological - genetics Toxins, Biological - metabolism Toxins, Biological - pharmacology Viscum album - chemistry Viscum album coloratum |
Title | Molecular Characterization of the Recombinant A-chain of a Type Ⅱ Ribosome-Inactivating Protein (RIP) from Viscum album coloratum and Structural Basis on its Ribosome-Inactivating Activity and the Sugar-binding Properties of the B-chain |
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