Orengo C A, Taylor W R
Laboratory of Mathematical Biology, National Institute for Medical Research, Mill Hill, London, U.K.
J Mol Biol. 1993 Oct 5;233(3):488-97. doi: 10.1006/jmbi.1993.1526.
A method for the comparison of protein three-dimensional substructures was developed. The method employs the double dynamic programming method of Taylor & Orengo but identifies multiple local alignments rather than a single global alignment. A modification based on the Smith Waterman algorithm for sequence alignment enables the automatic identification and growth of the most structurally similar local alignments irrespective of length and composition. The method can also be used in a search mode to match substructures. Roughly five minutes is required to find all Greek-key motifs in a protein of 100 residues. Two novel globin folds have been detected using the method, the antibiotic protein colicin A and diphtheria toxin, neither of which have any functional relationship to the globins.
开发了一种用于比较蛋白质三维子结构的方法。该方法采用了泰勒和奥伦戈的双重动态规划方法,但识别的是多个局部比对而非单个全局比对。基于史密斯-沃特曼序列比对算法的一种改进,能够自动识别并拓展结构上最相似的局部比对,而无需考虑长度和组成。该方法也可用于搜索模式以匹配子结构。在一个含有100个残基的蛋白质中找到所有希腊钥匙模体大约需要五分钟。使用该方法检测到了两种新的珠蛋白折叠结构,抗生素蛋白大肠杆菌素A和白喉毒素,它们与珠蛋白均无任何功能关联。