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The 3-D Structure of Crystal Protein Parasporin-2 that is Non-hemolytic but Capable of Preferentially Killing Cancer Cells

LIN Yi,ZHANG Tong-wu,CHEN Zhi-shan,CAI Fu-ying(Department of Bioengineering & Biotechnology,Huaqiao University,Key Laboratory of Industrial Biotechnology of Fujian Province University, Quanzhou 362021,Fujian,China)  
The initial three dimensional structure of Parasporin-2(Cry46Aa1)was constructed by homology modeling method,then was optimized by molecular mechanics method.The quality of the structure was evaluated to be good using Ramachandran plot and structural matching.In addition,the structural difference between Cry46Aa1 and Cry46Ab1 was presented.The interaction between Parasporin-2 and its receptor,GPI-anchored protein(CD59),was simulated using macromolecular docking procedures Hex4.5.It showed that the residues in a groove below two α-helixs of Parasporin-2 were responsible for the interaction,and the four loops of CD59 inserted the groove.The results provided a basis for the rational design of Cry46Aa1,and help us to understand the interactions between Cry46Aa1 and cellular receptor.
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