Jones S, Thornton J M
Department of Biochemistry and Molecular Biology, University College, Gower Street, London, WC1E 6BT, England.
J Mol Biol. 1997 Sep 12;272(1):121-32. doi: 10.1006/jmbi.1997.1234.
Protein-protein interaction sites in complexes of known structure are characterised using a series of parameters to evaluate what differentiates them from other sites on the protein surface. Surface patches are defined in protomers from a data set of 28 homo-dimers, 20 different hetero-complexes (segregated into large and small protomers), and antigens from six antibody-antigen complexes. Six parameters (solvation potential, residue interface propensity, hydrophobicity, planarity, protrusion and accessible surface area) are calculated for the observed interface patch and all other surface patches defined on each protein. A ranking of the observed interface, relative to all other possible patches, is calculated. With this approach it becomes possible to analyse the distribution of the rankings of all the observed patches, relative to all other surface patches, for each data set. For each type of complex, none of the parameters were definitive, but the majority showed trends for the observed interface to be distinguished from other surface patches.
利用一系列参数对已知结构复合物中的蛋白质-蛋白质相互作用位点进行表征，以评估它们与蛋白质表面其他位点的差异。表面斑块是从28个同二聚体、20个不同的异源复合物（分为大的和小的原体）以及6个抗体-抗原复合物的抗原的数据集中的原体中定义的。针对观察到的界面斑块以及在每个蛋白质上定义的所有其他表面斑块，计算六个参数（溶剂化势、残基界面倾向、疏水性、平面性、突出度和可及表面积）。计算观察到的界面相对于所有其他可能斑块的排名。通过这种方法，就有可能分析每个数据集中所有观察到的斑块相对于所有其他表面斑块的排名分布。对于每种类型的复合物，没有一个参数是决定性的，但大多数参数显示出观察到的界面与其他表面斑块有区别的趋势。
