A heptad motif of leucine residues found in membrane proteins can drive self-assembly of artificial transmembrane segments.

@article{Gurezka1999AHM,
  title={A heptad motif of leucine residues found in membrane proteins can drive self-assembly of artificial transmembrane segments.},
  author={Rolf Gurezka and Rico Laage and B Brosig and Dieter Langosch},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 14},
  pages={9265-70}
}
Specific interactions between alpha-helical transmembrane segments are important for folding and/or oligomerization of membrane proteins. Previously, we have shown that most transmembrane helix-helix interfaces of a set of crystallized membrane proteins are structurally equivalent to soluble leucine zipper interaction domains. To establish a simplified model of these membrane-spanning leucine zippers, we studied the homophilic interactions of artificial transmembrane segments using different… CONTINUE READING