Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/95124
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
Authors: Kang, Cong Bao
Ye, Wen-Hui
Nanga, Ravi Prakash Reddy
Song, Joo-Hye
Song, Seong Kyu
Yoon, Ho Sup
Keywords: DRNTU::Science::Biological sciences::Microbiology
Issue Date: 2006
Source: Ye, W., Nanga, R. P. R., Kang, C. B., Song, J. H., Song, S. K., & Yoon, H. S. (2006). 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. Journal of Biochemistry and Molecular Biology, 39(5), 560-570.
Series/Report no.: Journal of biochemistry and molecular biology
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 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.
URI: https://hdl.handle.net/10356/95124
http://hdl.handle.net/10220/8824
Rights: © 2006 Springer Verlag. This is the author created version of a work that has been peer reviewed and accepted for publication by Journal of Biochemistry and Molecular Biology, Springer Verlag. It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document. The published version is available at: [http://www.jbmb.or.kr/fulltext/jbmb/view.php?vol=39&page=560 ]
metadata.item.grantfulltext: open
metadata.item.fulltext: With Fulltext
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