6533b874fe1ef96bd12d63cf
RESEARCH PRODUCT
Transmembrane helix–helix interactions are modulated by the sequence context and by lipid bilayer properties
Florian CymerDirk SchneiderAnbazhagan Veerappansubject
Models MolecularLateral pressureLipid BilayersMolecular Sequence DataBiophysicsModels BiologicalBiochemistryProtein Structure SecondaryProtein structureAmino Acid SequenceLipid bilayerHydrogen bondGxxxGChemistryHydrogen bondMembrane ProteinsHydrophobic thicknessCell BiologyTransmembrane proteinTransmembrane domainCrystallographyMembraneMembrane proteinMembrane proteinBiophysicsProtein foldingHelix dimerProtein Bindingdescription
Abstract Folding of polytopic transmembrane proteins involves interactions of individual transmembrane helices, and multiple TM helix–helix interactions need to be controlled and aligned to result in the final TM protein structure. While defined interaction motifs, such as the GxxxG motif, might be critically involved in transmembrane helix–helix interactions, the sequence context as well as lipid bilayer properties significantly modulate the strength of a sequence specific transmembrane helix–helix interaction. Structures of 11 transmembrane helix dimers have been described today, and the influence of the sequence context as well as of the detergent and lipid environment on a sequence specific dimerization is discussed in light of the available structural information. This article is part of a Special Issue entitled: Protein Folding in Membranes.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2012-04-01 | Biochimica et Biophysica Acta (BBA) - Biomembranes |