Membrane protein assembly patterns reflect selection for non-proliferative structures

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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. © 2007 Federation of European Biochemical Societies.




Rath, A., & Deber, C. M. (2007). Membrane protein assembly patterns reflect selection for non-proliferative structures. FEBS Letters, 581(7), 1335–1341.

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