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Membrane protein folding: beyond the two stage model.

Donald M Engelman·Yang Chen·Chen-Ni Chin·A Rachael Curran·Ann M Dixon·Allison D Dupuy·Albert S Lee·Ursula Lehnert·Erin E Matthews·Yana K Reshetnyak·Alessandro Senes·Jean-Luc Popot
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Abstract

The folding of alpha-helical membrane proteins has previously been described using the two stage model, in which the membrane insertion of independently stable alpha-helices is followed by their mutual interactions within the membrane to give higher order folding and oligomerization. Given recent advances in our understanding of membrane protein structure it has become apparent that in some cases the model may not fully represent the folding process. Here we present a three stage model which gives considerations to ligand binding, folding of extramembranous loops, insertion of peripheral domains and the formation of quaternary structure.

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AquaporinsBacterial ProteinsBacteriorhodopsinsBinding SitesEscherichia coli ProteinsLigandsLipid BilayersMembrane ProteinsModels, MolecularPotassium ChannelsProtein FoldingProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryThermodynamicsJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.Review

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Donald M Engelman, Yang Chen, Chen-Ni Chin, A Rachael Curran, Ann M Dixon, Allison D Dupuy, Albert S Lee, Ursula Lehnert, Erin E Matthews, Yana K Reshetnyak, Alessandro Senes, Jean-Luc Popot. 2003-11-27. Membrane protein folding: beyond the two stage model.. https://doi.org/10.1016/s0014-5793(03)01106-2

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