Protein fold similarity estimated by a probabilistic approach based on Cα-Cα distance comparison
Protein fold similarity estimated by a probabilistic approach based on Cα-Cα distance comparison
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DOI：
10.1006/jmbi.2001.5250
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发表时间：
2002-01-25
影响因子：
5.6
通讯作者：
Pongor, S
中科院分区：
文献类型：
--
作者：
Carugo, O;Pongor, S
由3到30个氨基酸残基分隔的残基之间的C-α-C-α距离的分布是蛋白质折叠的高度特征，这使得通过直接比较距离直方图来识别它们是可能的。通过列联表分析进行比较，得到相同的概率(骄傲分数)，值在0到1之间。对于密切相关的结构，骄傲与C-α原子之间的均方根距离高度相关，但它提供了正确的分类，即使对于结构比对没有意义的无关结构也是如此。例如，对Cath折叠结构数据库的分析表明，根据获得的最高骄傲分数，98.8%的折叠属于正确的Cath同源超家族类别。结构比对和二级结构分配不是计算Pride所必需的，它的速度足够快，可以扫描大型数据库。(C)2002年学术出版社。
The distribution of the C-alpha-C-alpha distances between residues separated by three to 30 amino acid residues is highly characteristic of protein folds and makes it possible to identify them from a straightforward comparison of the distance histograms. The comparison is carried out by contingency table analysis and yields a probability of identity (PRIDE score), with values between zero and 1. For closely related structures, PRIDE is highly correlated with the root-mean-square distance between C-alpha atoms, but it provides a correct classification even for unrelated structures for which a structural alignment is not meaningful. For example, an analysis of the CATH database of fold structures showed that 98.8 % of the folds fall into the correct CATH homologous superfamily category, based on the highest PRIDE score obtained. Structural alignment and secondary-structure assignment are not necessary for the calculation of PRIDE, which is fast enough to allow the scanning of large databases. (C) 2002 Academic Press.