COMPARISON OF CONFORMATIONAL CHARACTERISTICS IN STRUCTURALLY SIMILAR PROTEIN PAIRS
COMPARISON OF CONFORMATIONAL CHARACTERISTICS IN STRUCTURALLY SIMILAR PROTEIN PAIRS
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DOI：
10.1002/pro.5560021104
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发表时间：
1993-11-01
期刊：
影响因子：
8
通讯作者：
THORNTON, JM
中科院分区：
文献类型：
--
作者：
FLORES, TP;ORENGO, CA;THORNTON, JM
虽然它是已知的，三维结构是很好的保守在蛋白质的进化发展过程中，有很少的研究，考虑其他参数除了分歧的主链坐标。在这项研究中，我们比对了90对同源蛋白质的结构，其序列同一性范围从5到100%。它们的结构进行了比较，作为一个功能的序列同一性，不仅包括考虑Calpha坐标，但也可访问性，Ooi数，二级结构，和侧链角度。我们将讨论这些属性如何改变的序列变得不太相似。这将在同源建模中具有实际用途，特别是对于建模非常遥远的相关或类似的蛋白质。我们还考虑了插入和缺失的平均大小和数量如何随着序列的不同而变化。这项研究提供了进一步的定量证据，表明结构在细节上以及在拓扑水平上是非常保守的，即使序列没有显示出统计学上显著的相似性。
Although it is known that three-dimensional structure is well conserved during the evolutionary development of proteins, there have been few studies that consider other parameters apart from divergence of the main-chain coordinates. In this study, we align the structures of 90 pairs of homologous proteins having sequence identities ranging from 5 to 100%. Their structures are compared as a function of sequence identity, including not only consideration of Calpha coordinates but also accessibility, Ooi numbers, secondary structure, and side-chain angles. We discuss how these properties change as the sequences become less similar. This will be of practical use in homology modeling, especially for modeling very distantly related or analogous proteins. We also consider how the average size and number of insertions and deletions vary as sequences diverge. This study presents further quantitative evidence that structure is remarkably well conserved in detail, as well as at the topological level, even when the sequences do not show similarity that is significant statistically.