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The machine that is a cell is more than the sum of its protein parts. A large step toward understanding how those parts are so effectively put together has been taken by Patrick Aloy, Rob Russell (EMBL, Heidelberg, Germany), and colleagues. Their work has identified ∼100 yeast protein complexes and predicted interactions within and among many of them.
EM data (gray) and known structures of a chaperonin (gold) and its inhibitors (red) help build a model for the full complex.
Russell/AAAS
“We were working on a large scale to model as many complexes as possible,” says Aloy. Proteins that purified together were assigned to functional groups. The authors built three-dimensional models for as many proteins in these groups as possible, based on known structures and protein homologies. They then predicted which proteins interact directly, and subsequently modeled the structures of complexes containing multiple proteins.
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The Rockefeller University Press
2004
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