Institute of Bioinformatics and Structural Biology, National Tsing Hua University, Hsinchu 30013, Taiwan.
Genome Biol. 2008 Jan 18;9(1):R11. doi: 10.1186/gb-2008-9-1-r11.
Circular permutation of a protein can be visualized as if the original amino- and carboxyl termini were linked and new ones created elsewhere. It has been well-documented that circular permutants usually retain native structures and biological functions. Here we report CPSARST (Circular Permutation Search Aided by Ramachandran Sequential Transformation) to be an efficient database search tool. In this post-genomics era, when the amount of protein structural data is increasing exponentially, it provides a new way to rapidly detect novel relationships among proteins.
环状排列的蛋白质可以通过将原始的氨基和羧基末端连接起来,并在其他地方创造新的末端来可视化。已经有充分的文献记载表明,环状变体通常保留天然结构和生物功能。在这里,我们报告 CPSARST(通过 Ramachandran 顺序变换辅助的环状排列搜索)是一种有效的数据库搜索工具。在后基因组时代,当蛋白质结构数据的数量呈指数级增长时,它为快速检测蛋白质之间的新关系提供了一种新方法。