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同源蛋白结构建模的进展。

Advances in homology protein structure modeling.

作者信息

Xiang Zhexin

机构信息

Center for Molecular Modeling, Center for Information Technology, National Institutes of Health, Building 12A Room 2051, 12 South Drive, Bethesda, Maryland 20892-5624, USA.

出版信息

Curr Protein Pept Sci. 2006 Jun;7(3):217-27. doi: 10.2174/138920306777452312.

Abstract

Homology modeling plays a central role in determining protein structure in the structural genomics project. The importance of homology modeling has been steadily increasing because of the large gap that exists between the overwhelming number of available protein sequences and experimentally solved protein structures, and also, more importantly, because of the increasing reliability and accuracy of the method. In fact, a protein sequence with over 30% identity to a known structure can often be predicted with an accuracy equivalent to a low-resolution X-ray structure. The recent advances in homology modeling, especially in detecting distant homologues, aligning sequences with template structures, modeling of loops and side chains, as well as detecting errors in a model, have contributed to reliable prediction of protein structure, which was not possible even several years ago. The ongoing efforts in solving protein structures, which can be time-consuming and often difficult, will continue to spur the development of a host of new computational methods that can fill in the gap and further contribute to understanding the relationship between protein structure and function.

摘要

同源建模在结构基因组学项目中确定蛋白质结构方面发挥着核心作用。由于可用蛋白质序列的数量与通过实验解析的蛋白质结构数量之间存在巨大差距,而且更重要的是,由于该方法的可靠性和准确性不断提高,同源建模的重要性一直在稳步增加。事实上,与已知结构具有超过30%同一性的蛋白质序列通常可以以等同于低分辨率X射线结构的准确性进行预测。同源建模的最新进展,特别是在检测远源同源物、将序列与模板结构比对、环和侧链建模以及检测模型中的错误方面,有助于可靠地预测蛋白质结构,而这在几年前甚至是不可能的。解决蛋白质结构的持续努力可能既耗时又往往困难,这将继续推动一系列新的计算方法的发展,这些方法可以填补空白,并进一步有助于理解蛋白质结构与功能之间的关系。

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