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J Mol Biol. 1997 Sep 12;272(1):121-32.

Analysis of protein-protein interaction sites using surface patches.

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Department of Biochemistry and Molecular Biology, University College, Gower Street, London, WC1E 6BT, England.


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.

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