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- Title
Membrane protein assembly patterns reflect selection for non-proliferative structures
- Authors
Rath, Arianna; Deber, Charles M.
- Abstract
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.
- Subjects
MEMBRANE proteins; MATHEMATICAL complexes; PROTEIN folding; BIOMOLECULES
- Publication
FEBS Letters, 2007, Vol 581, Issue 7, p1335
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2007.02.050