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• W2128796532 abstract "Deciphering the whole network of protein interactions for a given proteome ('interactome') is the goal of many experimental and computational efforts in Systems Biology. Separately the prediction of the structure of protein complexes by docking methods is a well-established scientific area. To date, docking programs have not been used to predict interaction partners. We provide a proof of principle for such an approach. Using a set of protein complexes representing known interactors in their unbound form, we show that a standard docking program can distinguish the true interactors from a background of 922 non-redundant potential interactors. We additionally show that true interactions can be distinguished from non-likely interacting proteins within the same structural family. Our approach may be put in the context of the proposed 'funnel-energy model'; the docking algorithm may not find the native complex, but it distinguishes binding partners because of the higher probability of favourable models compared with a collection of non-binders. The potential exists to develop this proof of principle into new approaches for predicting interaction partners and reconstructing biological networks." @default.
• W2128796532 created "2016-06-24" @default.
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• W2128796532 date "2011-01-01" @default.
• W2128796532 modified "2023-10-17" @default.
• W2128796532 title "Towards the prediction of protein interaction partners using physical docking" @default.
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• W2128796532 doi "https://doi.org/10.1038/msb.2011.3" @default.
• W2128796532 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3063693" @default.
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