Send to

Choose Destination
See comment in PubMed Commons below
Biochim Biophys Acta. 2012 Apr;1818(4):963-73. doi: 10.1016/j.bbamem.2011.07.035. Epub 2011 Jul 31.

Transmembrane helix-helix interactions are modulated by the sequence context and by lipid bilayer properties.

Author information

  • 1Institut für Pharmazie und Biochemie, Johannes Gutenberg-Universität Mainz, Johann-Becher-Weg 30, 55128 Mainz, Germany.


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.

Copyright © 2011 Elsevier B.V. All rights reserved.

[PubMed - indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk