Jones, S; Thornton, JM; (1997) Prediction of protein-protein interaction sites using patch analysis. J Mol Biol , 272 (1) 133 - 143. 10.1006/jmbi.1997.1233.
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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.
|Title:||Prediction of protein-protein interaction sites using patch analysis.|
|Keywords:||Antigens, Binding Sites, Dimerization, Protein Binding, Proteins, Surface Properties|
|UCL classification:||UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of)|
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