title: Transmembrane helix-helix interactions are modulated by the sequence context and by lipid bilayer properties.
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.
authors.affiliation: Institut für Pharmazie und Biochemie, Johannes Gutenberg-Universität Mainz, Johann-Becher-Weg 30, 55128 Mainz, Germany.
authors.forename: Florian
authors.initials: F
authors.lastname: Cymer
authors.forename: Anbazhagan
authors.initials: A
authors.lastname: Veerappan
authors.forename: Dirk
authors.initials: D
authors.lastname: Schneider
mesh_terms: D000595:Amino Acid Sequence; D008051:Lipid Bilayers / Q000737:chemistry*; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D017433:Protein Structure, Secondary
chemical_list: D008051:Lipid Bilayers; D008565:Membrane Proteins