Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1818, Issue 4, Pages 963-973Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2011.07.035
Keywords
Membrane protein; Helix dimer; GxxxG; Hydrogen bond; Lateral pressure; Hydrophobic thickness
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Funding
- Stiftung Rheinland-Pfalz fur Innovation
- Deutsche Forschungsgemeinschaft [SCHN 690/2-3, GRK 1478]
- German-Israeli Foundation
- Centre of Complex Matter (COMATT)
- University of Mainz
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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. (C) 2011 Elsevier B.V. All rights reserved.
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