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- W2078166105 abstract "Membrane proteins that regulate solute movement are often built from multiple copies of an identical polypeptide chain. These complexes represent striking examples of self-assembling systems that recruit monomers only until a prescribed level for function is reached. Here we report that three modes of assembly – distinguished by sequence and stoichiometry – describe all helical membrane protein complexes currently solved to high resolution. Using the 13 presently available non-redundant homo-oligomeric structures, we show that two of these types segregate with protein function: one produces energy-dependent transporters, while the other builds channels for passive diffusion. Given such limited routes to functional complexes, membrane proteins that self-assemble exist on the edge of aggregation, susceptible to mutations that may underlie human diseases." @default.
- W2078166105 created "2016-06-24" @default.
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- W2078166105 date "2007-03-01" @default.
- W2078166105 modified "2023-10-12" @default.
- W2078166105 title "Membrane protein assembly patterns reflect selection for non-proliferative structures" @default.
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- W2078166105 doi "https://doi.org/10.1016/j.febslet.2007.02.050" @default.
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