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):133-43. doi: 10.1006/jmbi.1997.1233.
A method for defining and analysing a series of residue patches on the surface of protein structures is used to predict the location of protein-protein interaction sites. Each residue patch is analysed for six parameters; solvation potential, residue interface propensity, hydrophobicity, planarity, protrusion and accessible surface area. The method involves the calculation of a relative combined score that gives the probability of a surface patch forming protein-protein interactions. Predictions are made for the known structures of protomers from 28 homo-dimers, large protomers from 11 hetero-complexes, small protomers from 14 hetero-complexes, and antigens from six antibody-antigen complexes. The predictions are successful for 66% (39/59) of the structures and the remainder can usually be rationalized in terms of additional interaction sites.
一种用于定义和分析蛋白质结构表面一系列残基斑块的方法被用于预测蛋白质-蛋白质相互作用位点的位置。对每个残基斑块分析六个参数：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。该方法涉及计算一个相对综合得分，该得分给出表面斑块形成蛋白质-蛋白质相互作用的概率。对来自28个同二聚体的原体已知结构、来自11个异源复合物的大原体、来自14个异源复合物的小原体以及来自6个抗体-抗原复合物的抗原进行了预测。对于66%（39/59）的结构预测是成功的，其余的通常可以根据额外的相互作用位点进行合理说明。
