Comprehensive statistical analysis of residues interaction specificity at protein-protein interfaces
Comprehensive statistical analysis of residues interaction specificity at protein-protein interfaces
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DOI：
10.1002/prot.21363
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发表时间：
2007-06-01
影响因子：
2.9
通讯作者：
Tumanyan, Vladimir
中科院分区：
文献类型：
--
作者：
Anashkina, Anastasya;Kuznetsov, Eugene;Tumanyan, Vladimir
我们使用无偏Voronoi-Delaune Tessellation方法在原子水平上计算了4602个非冗余蛋白质-蛋白质界面的链间接触，并对同源二聚体和杂合物制作了20 × 20残基接触矩阵。接触的面积和这些接触的距离分布计算上的残留物和原子水平。我们分析了残留面积分布，并显示存在两种类型的残留间接触：随机的和特定的。我们还推导出公式描述的随机和特定的相互作用的参数形式的接触面积的分布。发现Cys-Cys接触和带相反电荷的相互作用的最大配对偏好指数。观察到同源二聚体和杂合物之间的残基接触的显着差异。由于结构对称性的影响，同二聚体中的界面富含相同类型的残基之间的接触。Proteins 2007;67：1060-1077. (C)2007 Wiley-Liss，Inc.
We calculated interchain contacts on the atomic level for nonredundant set of 4602 protein-protein interfaces using an unbiased Voronoi-Delaune tessellation method, and made 20X20 residue contact matrixes both for homodimers and heterocomplexes. The area of contacts and the distance distribution for these contacts were calculated on both the residue and the atomic levels. We analyzed residue area distribution and showed the existence of two types of interresidue contacts: stochastic and specific. We also derived formulas describing the distribution of contact area for stochastic and specific interactions in parametric form. Maximum pairing preference index was found for Cys-Cys contacts and for oppositely charged interactions. A significant difference in residue contacts was observed between homodimers and heterocomplexes. Interfaces in homodimers were enriched with contacts between residues of the same type due to the effects of structure symmetry. Proteins 2007;67:1060-1077. (C) 2007 Wiley-Liss, Inc.