Interaction and conformational dynamics of membrane-spanning protein helices

Dieter Langosch*, Isaiah T. Arkin

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

98 Scopus citations

Abstract

Within 1 or 2 decades, the reputation of membrane-spanning α-helices has changed dramatically. Once mostly regarded as dull membrane anchors, transmembrane domains are now recognized as major instigators of protein-protein interaction. These interactions may be of exquisite specificity in mediating assembly of stable membrane protein complexes from cognate subunits. Further, they can be reversible and regulatable by external factors to allow for dynamic changes of protein conformation in biological function. Finally, these helices are increasingly regarded as dynamic domains. These domains can move relative to each other in different functional protein conformations. In addition, small-scale backbone fluctuations may affect their function and their impact on surrounding lipid shells. Elucidating the ways by which these intricate structural features are encoded by the amino acid sequences will be a fascinating subject of research for years to come.

Original languageAmerican English
Pages (from-to)1343-1358
Number of pages16
JournalProtein Science
Volume18
Issue number7
DOIs
StatePublished - Jul 2009

Keywords

  • Assembly
  • Dynamics
  • Interaction
  • Membrane protein
  • Transmembrane helix

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