ob -折叠Π-modules氨基酸序列的结构与特征

E. Brazhnikov, A. V. Efimov
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引用次数: 0

摘要

对含有OB-fold的大量非同源蛋白结构П-modules进行了立体化学分析。该模块由两条β链组成,由一个环连接,并以一种看起来像希腊字母П的方式放置在不同的薄片上。从属于16个OB-fold超家族的265个合适结构中选择了70个分辨率不小于2.5Å的非同源蛋白进行分析。我们公开了两种类型的П-modules:第一种是含有α-螺旋的连接环,第二种是没有螺旋的连接环。蛋白链进入第二β-片的构象为βββαLβp。在大多数情况下,85%的α-位置被甘氨酸残基占据,而在环的入口处不存在这些残基。得到了П-modules的占用频率与回路长度的关系。各模块结构的空间路径叠加良好。П-module序列的氨基酸结构比对使我们能够确定疏水、亲水性和甘氨酸残基的关键位置。
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Structure and features of amino acid sequences of Π-modules in OB-folds
Stereochemical analysis has been performed for П-modules from the large set of non-homologous protein structures containing the OB-fold. That module consists of two β-strands connected by a loop and placed in different sheets in such a way which looks as Greek letter П. Total 70 non-homologous proteins at resolution not less than 2.5Å have been selected for the analysis from 265 suitable structures belonging to sixteen OB-fold super families. We have disclosed two types of П-modules: the fist with the connecting loop containing α-helix, and second one without helix. Entrance of protein chain into second β-sheet is carried out by the same arch with conformation βββαLβp. In most cases, 85 % of total, α-positions are occupied by glycine residue, while at entrance in the loop such residues are absent. Occupancy frequency of П-modules has been obtained in dependence on the loop length. Spatial pathway of structures of all modules are superimposed very well. Structural alignment of amino acid for П-module sequences allows us to determine the key positions of the hydrophobic, hydrophilic, and glycine residues.
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来源期刊
Mathematical Biology and Bioinformatics
Mathematical Biology and Bioinformatics Mathematics-Applied Mathematics
CiteScore
1.10
自引率
0.00%
发文量
13
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