Elucidation of the Principles of Membrane Protein Folding Using Model Transmembrane Helices.

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Hydrophobic lipid bilayer environment constrains transmembrane proteins mostly into an α-helical bundle structure. The folding processes of α-helical transmembrane proteins can be understood in terms of two energetically distinct stages, i.e. 1) independently stable transmembrane helices are formed and 2) the helices interact with each other to give a functional protein. The simplicity of the folding process enables us to use model transmembrane helices for elucidating driving forces working in membrane protein folding in the context of helix-helix interactions. Recent studies have devised several appropriate model peptides that form stable transmembrane helices and just started to quantitatively measure the helix-helix interactions in lipid bilayers. Possible driving forces involved in helix-helix and helix-lipid interactions are summarized. Statistical analyses of structure-known membrane proteins indicate diverse driving forces including the leucine zipper, the GlyXXXGly motif, network of hydrogen bonds and salt bridge.Furthermore, the lipid bilayer environment, which consists of diverse lipid species with asymmetric distributions in inner and outer leaflets, should have substantial effects on helix-helix interactions, therefore on the conformations of the whole proteins.
日本膜学会の論文

著者

矢野義明
京都大学大学院生命科学研究科システム機能学分野

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