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. 2011 Jan 4:165–186. doi: 10.1007/978-3-7091-0045-5_10

Helix-helix interaction patterns in membrane proteins

Dieter Langosch 2, Jana R Herrmann 2, Stephanie Unterreitmeier 2, Angelika Fuchs 3
PMCID: PMC7123687

Abstract

Membrane-spanning α-helices represent major sites of protein-protein interaction in membrane protein oligomerization and folding. As such, these interactions may be of exquisite specificity. Specificity often rests on a complex interplay of different types of residues forming the helix-helix interfaces via dense packing and different non-covalent forces, including van der Waal’s forces, hydrogen bonding, charge-charge interactions, and aromatic interactions. These interfaces often contain complex residue motifs where the contribution of constituent amino acids depends on the context of the surrounding sequence. Moreover, transmembrane helix-helix interactions are increasingly recognized as being dynamic and dependent on the functional state of a given protein.

Abbreviations: GpA, glycophorin A; H-bond, hydrogen bond; TMD, transmembrane domain

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