X-ray sequence and crystal structure of luffaculin 1, a novel type 1 ribosome-inactivating protein |
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| Authors: | Xiaomin Hou Minghuang Chen Liqing Chen Edward J Meehan Jieming Xie Mingdong Huang |
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| Affiliation: | (1) State Key Laboratory of Structural Chemistry, Fujian Institute of Research on the Structure of Matter, The Chinese Academy of Sciences, 155 Yang Qiao Xi Lu, Fuzhou, Fujian, 350002, China;(2) Graduate School of Chinese Academy of Sciences, The Chinese Academy of Sciences, Beijing, 10039, China;(3) Laboratory for Structural Biology, Department of Chemistry, Graduate Programs of Biotechnology, Chemistry and Materials Science, University of Alabama in Huntsville, Huntsville, AL 35899, USA;(4) Fujian Medical University, Fuzhou, 350004, China |
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| Abstract: | Background Protein sequence can be obtained through Edman degradation, mass spectrometry, or cDNA sequencing. High resolution X-ray crystallography can also be used to derive protein sequence information, but faces the difficulty in distinguishing the Asp/Asn, Glu/Gln, and Val/Thr pairs. Luffaculin 1 is a new type 1 ribosome-inactivating protein (RIP) isolated from the seeds of Luffa acutangula. Besides rRNA N-glycosidase activity, luffaculin 1 also demonstrates activities including inhibiting tumor cells' proliferation and inducing tumor cells' differentiation. |
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