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A dimerization motif for transmembrane α–helices

Nature Structural Biology volume 1, pages 157–163 (1994)Cite this article

Abstract

Specific helix–helix interactions inside lipid bilayers guide the folding and assembly of many integral membrane proteins and their complexes. We report here a pattern of 7 amino acids (LIxxGVxxGVxxT) which when introduced into several hydrophobic transmembrane α–helices promotes their specific dimerization. Dimerization is driven by interactions that are specific, dominated by the helix–helix interface, and involve no potentially ionizable groups. The motif may provide a useful tool for the functional analysis of such interactions in a variety of systems. Further, since this particular motif is rare, whilst specific helix association is not, many other such motifs may exist, which could permit sorting within complex membranes as well as guiding folding and oligomerization.

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Author information

Author notes

  1. Mark A. Lemmon

    Present address: Department of Pharmacology, New York University Medical Center, 550 First Avenue, New York, NY, 10016, USA

  2. Herbert R. Treutlein

    Present address: Ludwig Institute for Cancer Research, P.O. Royal Melbourne Hospital, Parkville, Victoria, 3050, Australia

Authors and Affiliations

  1. Department of Molecular Biophysics & Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT, 06520, USA

    Mark A. Lemmon, Herbert R. Treutlein, Paul D. Adams, Axel T. Brünger & Donald M. Engelman

  2. Howard Hughes Medical Institute, Yale University, 266 Whitney Avenue, New Haven, CT, 06520, USA

    Herbert R. Treutlein & Axel T. Brünger

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  1. Mark A. Lemmon
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  5. Donald M. Engelman
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Lemmon, M., Treutlein, H., Adams, P. et al. A dimerization motif for transmembrane α–helices. Nat Struct Mol Biol 1, 157–163 (1994). https://doi.org/10.1038/nsb0394-157

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