Journal
MOLECULAR SYSTEMS BIOLOGY
Volume 7, Issue -, Pages -Publisher
WILEY
DOI: 10.1038/msb.2011.3
Keywords
interactome; protein docking; protein-protein interaction
Categories
Funding
- British Council Research
- Marie Curie Action European Reintegration [MERG-CT-2007-200179]
- BioSapiens Network of Excellence [LSHG-CT-2003-503265]
- Spanish Ministry for Education and Science
Ask authors/readers for more resources
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. Molecular Systems Biology 7: 469; published online 15 February 2011; doi: 10.1038/msb.2011.3
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available